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Cavarelli J, Moras D. Recognition of tRNAs by aminoacyl-tRNA synthetases. FASEB J. 7:1993;79-86.
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0028812785
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Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog
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of outstanding interest. The first crystal structure of the ternary complex of EF-Tu is presented. It reveals details of the tRNA binding that are different to those predicted from many biochemical results. The unexpected similarity of EF-Tu compared with the structure of EF-G-GDP, implies macromolecular mimicry. This has important implications for the function of the ribosome and for the evolution of translation factors.
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Nissen P, Kjeldgaard M, Thirup S, Polekhina G, Reshetnikova L, Clark BFC, Nyborg J. Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog. of outstanding interest Science. 270:1995;1464-1472 The first crystal structure of the ternary complex of EF-Tu is presented. It reveals details of the tRNA binding that are different to those predicted from many biochemical results. The unexpected similarity of EF-Tu compared with the structure of EF-G-GDP, implies macromolecular mimicry. This has important implications for the function of the ribosome and for the evolution of translation factors.
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Science
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Nissen, P.1
Kjeldgaard, M.2
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Clark, B.F.C.6
Nyborg, J.7
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Recognition of aminoacyl-tRNAs by protein elongation factors
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S. Söll, RajBhandary U. Washington: American Society for Microbiology Press
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Clark BFC, Kjeldgaard M, Barciszewski J, Sprinzl M. Recognition of aminoacyl-tRNAs by protein elongation factors. Söll S, RajBhandary U. tRNA: Structure, Biosynthesis and Function. 1995;423-442 American Society for Microbiology Press, Washington.
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TRNA: Structure, Biosynthesis and Function
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Clark, B.F.C.1
Kjeldgaard, M.2
Barciszewski, J.3
Sprinzl, M.4
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4
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0030584663
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A complex profile of protein elongation: Translating chemical energy into molecular movement
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of special interest. A review describing the ternary complex, molecular mimicry and EF-Tu-EF-Ts. A schematic view of one elongation and translocation cycle in prokaryotic protein biosynthesis is presented.
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Abel K, Jurnak F. A complex profile of protein elongation: translating chemical energy into molecular movement. of special interest Structure. 4:1996;229-238 A review describing the ternary complex, molecular mimicry and EF-Tu-EF-Ts. A schematic view of one elongation and translocation cycle in prokaryotic protein biosynthesis is presented.
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Structure
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Abel, K.1
Jurnak, F.2
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0029958571
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The GTP-binding motif - variations on a theme
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of special interest. A review on all presently known structures of GTP-binding proteins. It is shown that the switch regions behave differently, most probably reflecting different biological functions.
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Kjeldgaard M, Nyborg J, Clark BFC. The GTP-binding motif - variations on a theme. of special interest FASEB J. 10:1996;1347-1368 A review on all presently known structures of GTP-binding proteins. It is shown that the switch regions behave differently, most probably reflecting different biological functions.
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FASEB J
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Kjeldgaard, M.1
Nyborg, J.2
Clark, B.F.C.3
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Elongation in bacterial protein biosynthesis
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Nyborg J, Kjeldgaard M. Elongation in bacterial protein biosynthesis. Curr Opin Biotechnol. 7:1996;369-375.
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Curr Opin Biotechnol
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Nyborg, J.1
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0027394282
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Structural aspects of ribonucleoprotein interactions in ribosomes
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Yonath A, Franceschi F. Structural aspects of ribonucleoprotein interactions in ribosomes. Curr Opin Struct Biol. 3:1993;45-49.
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Curr Opin Struct Biol
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Yonath, A.1
Franceschi, F.2
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8
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0029100747
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A model of protein synthesis based on a new cryo-electron microscopy reconstruction of the E. coli ribosome
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of outstanding interest. The most detailed structural model of protein synthesis determined by cryo-EM until now is presented. Several new channels are seen in the model.
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Frank J, Zhu J, Penczek P, Li Y, Srivastava S, Vershoor A, Radermacher M, Grassucci R, Lata RK, Agrawal RK. A model of protein synthesis based on a new cryo-electron microscopy reconstruction of the E. coli ribosome. of outstanding interest Nature. 376:1995;441-444 The most detailed structural model of protein synthesis determined by cryo-EM until now is presented. Several new channels are seen in the model.
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Nature
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, pp. 441-444
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Frank, J.1
Zhu, J.2
Penczek, P.3
Li, Y.4
Srivastava, S.5
Vershoor, A.6
Radermacher, M.7
Grassucci, R.8
Lata, R.K.9
Agrawal, R.K.10
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9
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0029645318
-
The 70S Escherichia coli ribosome at 23 Å resolution: Fitting the ribosomal RNA
-
of outstanding interest. Another ribosome reconstruction from cryo-EM very similar to that presented in [8]. The fitting of helical sections of ribosomal RNA into the model is proposed.
-
Stark H, Müller F, Orlova EV, Schatz M, Dube P, Erdemir T, Zemlin F, Brimacombe R, Van Heel M. The 70S Escherichia coli ribosome at 23 Å resolution: fitting the ribosomal RNA. of outstanding interest Structure. 3:1995;815-821 Another ribosome reconstruction from cryo-EM very similar to that presented in [8]. The fitting of helical sections of ribosomal RNA into the model is proposed.
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(1995)
Structure
, vol.3
, pp. 815-821
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Stark, H.1
Müller, F.2
Orlova, E.V.3
Schatz, M.4
Dube, P.5
Erdemir, T.6
Zemlin, F.7
Brimacombe, R.8
Van Heel, M.9
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10
-
-
0030040661
-
Direct visualization of A-, P-, and E-site transfer RNAs in the Escherichia coli ribosome
-
of outstanding interest. Three tRNAs are seen sitting in the interface between the large and the small subunit of the ribosome. The A- and P-site tRNAs are close to each other at the anticodons and at the CCA end. The angle between the planes of these two tRNAs is larger than expected.
-
Agrawal RK, Penczek P, Grassucci RA, Li Y, Leith A, Nierhaus KH, Frank J. Direct visualization of A-, P-, and E-site transfer RNAs in the Escherichia coli ribosome. of outstanding interest Science. 271:1996;1000-1002 Three tRNAs are seen sitting in the interface between the large and the small subunit of the ribosome. The A- and P-site tRNAs are close to each other at the anticodons and at the CCA end. The angle between the planes of these two tRNAs is larger than expected.
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Science
, vol.271
, pp. 1000-1002
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Agrawal, R.K.1
Penczek, P.2
Grassucci, R.A.3
Li, Y.4
Leith, A.5
Nierhaus, K.H.6
Frank, J.7
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11
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0029643859
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The crystal structure of ribosomal protein L14 reveals an important organizational component of the translational apparatus
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Davies C, White SW, Ramakrishnan V. The crystal structure of ribosomal protein L14 reveals an important organizational component of the translational apparatus. Structure. 4:1996;55-66.
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(1996)
Structure
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Davies, C.1
White, S.W.2
Ramakrishnan, V.3
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12
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9044249328
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Crystal structure of the RNA binding ribosomal protein L1 from Thermus thermophilus
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Nikonov S, Nevskaya N, Eliseikina I, Fomenkova N, Nikulin A, Ossina N, Garber M, Jonsson BH, Briand C, Al-Karadaghi S, et al. Crystal structure of the RNA binding ribosomal protein L1 from Thermus thermophilus. EMBO J. 15:1996;1350-1359.
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EMBO J
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Nikonov, S.1
Nevskaya, N.2
Eliseikina, I.3
Fomenkova, N.4
Nikulin, A.5
Ossina, N.6
Garber, M.7
Jonsson, B.H.8
Briand, C.9
Al-Karadaghi, S.10
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13
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0029608909
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Ribosomal proteins and elongation factors
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of special interest. A good review on the current status of the structural knowledge of ribosomal proteins and elongation factors. It is pointed out that the so-called 'split β-α-β' motif is found in six out of nine ribosomal proteins as well as in domain 5 of EF-G.
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Liljas A, Garber M. Ribosomal proteins and elongation factors. of special interest Curr Opin Struct Biol. 5:1995;721-727 A good review on the current status of the structural knowledge of ribosomal proteins and elongation factors. It is pointed out that the so-called 'split β-α-β' motif is found in six out of nine ribosomal proteins as well as in domain 5 of EF-G.
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Curr Opin Struct Biol
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Liljas, A.1
Garber, M.2
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14
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0028953727
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The sarcin/ricin loop, a modular RNA
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Szewczak AA, Moore PB. The sarcin/ricin loop, a modular RNA. J Mol Biol. 247:1995;81-98.
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Szewczak, A.A.1
Moore, P.B.2
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15
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Tyrosyl-tRNA synthetase forms a mononucleotide-binding fold
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Bhat TN, Blow DM, Brick P, Nyborg J. Tyrosyl-tRNA synthetase forms a mononucleotide-binding fold. J Mol Biol. 158:1982;699-709.
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Bhat, T.N.1
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Brick, P.3
Nyborg, J.4
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16
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0029127816
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Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate
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Arnez JG, Harris DC, Mitschler A, Rees B, Francklyn CS, Moras D. Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate. EMBO J. 14:1995;4143-4155.
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Arnez, J.G.1
Harris, D.C.2
Mitschler, A.3
Rees, B.4
Francklyn, C.S.5
Moras, D.6
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17
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0029091055
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Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus
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Logan DT, Mazauric MH, Kern D, Moras D. Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus. EMBO J. 14:1995;4156-4167.
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EMBO J
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Logan, D.T.1
Mazauric, M.H.2
Kern, D.3
Moras, D.4
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18
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0029165043
-
Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus
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Mosyak L, Reshetnikova L, Goldgur Y, Delarue M, Safro MG. Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus. Nat Struct Biol. 2:1995;537-547.
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Nat Struct Biol
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Mosyak, L.1
Reshetnikova, L.2
Goldgur, Y.3
Delarue, M.4
Safro, M.G.5
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19
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0028867140
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Crystallization of threonyl-tRNA synthetase from Thermus thermophilus and preliminary crystallographic data
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Cura V, Kern D, Mitschler A, Moras D. Crystallization of threonyl-tRNA synthetase from Thermus thermophilus and preliminary crystallographic data. FEBS Lett. 374:1995;110-112.
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FEBS Lett
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Cura, V.1
Kern, D.2
Mitschler, A.3
Moras, D.4
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20
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0029144604
-
Crystallisation of Thermus thermophilus histidyl-tRNA synthetase and its complex with tRNAHis
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Yaremchuk AD, Cusack S, Åberg A, Gudzera O, Kryklivyi I, Tukalo M. Crystallisation of Thermus thermophilus histidyl-tRNA synthetase and its complex with tRNAHis. Proteins. 22:1995;426-428.
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Proteins
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Yaremchuk, A.D.1
Cusack, S.2
Åberg, A.3
Gudzera, O.4
Kryklivyi, I.5
Tukalo, M.6
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21
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0024392753
-
Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA-Gln and ATP at 2.8 Å resolution
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Rould MA, Perona JJ, Söll D, Steitz TA. Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA-Gln and ATP at 2.8 Å resolution. Science. 246:1989;1135-1142.
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Science
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Rould, M.A.1
Perona, J.J.2
Söll, D.3
Steitz, T.A.4
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22
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0026429275
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Asp
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Asp. Science. 252:1991;1682-1689.
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(1991)
Science
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Ruff, M.1
Krishnaswamy, S.2
Breglin, M.3
Peterszman, A.4
Mitschler, A.5
Podjarny, A.6
Rees, B.7
Thierry, J.C.8
Moras, D.9
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24
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0027179878
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Crystal structure of active elongation factor Tu reveals major domain rearrangements
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Berchtold H, Reshetnikova L, Reiser COA, Schirmer NK, Sprinzl M, Hilgenfeld R. Crystal structure of active elongation factor Tu reveals major domain rearrangements. Nature. 365:1993;126-132.
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Nature
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Berchtold, H.1
Reshetnikova, L.2
Reiser, C.O.A.3
Schirmer, N.K.4
Sprinzl, M.5
Hilgenfeld, R.6
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25
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0027917990
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The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation
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Kjeldgaard M, Nissen P, Thirup S, Nyborg J. The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation. Structure. 1:1993;35-50.
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(1993)
Structure
, vol.1
, pp. 35-50
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Kjeldgaard, M.1
Nissen, P.2
Thirup, S.3
Nyborg, J.4
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26
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0028871610
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Interaction of guanosine nucleotides and their analogs with elongation factor Tu from Thermus thermophilus
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Wagner A, Simon I, Sprinzl M, Goody RS. Interaction of guanosine nucleotides and their analogs with elongation factor Tu from Thermus thermophilus. Biochemistry. 34:1995;12535-12542.
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Biochemistry
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, pp. 12535-12542
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Wagner, A.1
Simon, I.2
Sprinzl, M.3
Goody, R.S.4
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27
-
-
0030587857
-
Helix unwinding in the effector region of elongation factor EF-Tu·GDP
-
of special interest. The structure of intact EF-Tu·GDP is shown to be similar to that of proteolytically cleaved EF-Tu·GDP. The effector region shows a β hairpin where EF-Tu·GTP has a helix.
-
Polekhina G, Thirup S, Kjeldgaard M, Nissen P, Lippmann C, Nyborg J. Helix unwinding in the effector region of elongation factor EF-Tu·GDP. of special interest Structure. 4:1996;1141-1151 The structure of intact EF-Tu·GDP is shown to be similar to that of proteolytically cleaved EF-Tu·GDP. The effector region shows a β hairpin where EF-Tu·GTP has a helix.
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(1996)
Structure
, vol.4
, pp. 1141-1151
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Polekhina, G.1
Thirup, S.2
Kjeldgaard, M.3
Nissen, P.4
Lippmann, C.5
Nyborg, J.6
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28
-
-
0030017819
-
Limited hydrolysis and amino acid replacements in the effector region of Thermus thermophilus elongation factor Tu
-
of special interest. The structure in the vicinity of Glu56 and Arg59 in the effector region of EF-Tu is important for the control of the ribosome-induced GTPase activity.
-
Zeidler W, Schirmer NK, Egle C, Ribeiro S, Kreutzer R, Sprinzl M. Limited hydrolysis and amino acid replacements in the effector region of Thermus thermophilus elongation factor Tu. of special interest Eur J Biochem. 239:1996;265-271 The structure in the vicinity of Glu56 and Arg59 in the effector region of EF-Tu is important for the control of the ribosome-induced GTPase activity.
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(1996)
Eur J Biochem
, vol.239
, pp. 265-271
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Zeidler, W.1
Schirmer, N.K.2
Egle, C.3
Ribeiro, S.4
Kreutzer, R.5
Sprinzl, M.6
-
29
-
-
0030025671
-
The structure of the Escherichia coli EF-Tu·EF-Ts complex at 2.5 Å resolution
-
of outstanding interest. The structure of EF-Tu·EF-Ts completes the structural investigations of the EF-Tu cycle. The most important feature of the model is most probably that EF-Ts, by interacting with both domains 1 and 3 of EF-Tu, separates these domains to allow for the nucleotide exchange.
-
Kawashima T, Berthet-Colominas C, Wulff M, Cusack S, Leberman R. The structure of the Escherichia coli EF-Tu·EF-Ts complex at 2.5 Å resolution. of outstanding interest Nature. 379:1996;511-518 The structure of EF-Tu·EF-Ts completes the structural investigations of the EF-Tu cycle. The most important feature of the model is most probably that EF-Ts, by interacting with both domains 1 and 3 of EF-Tu, separates these domains to allow for the nucleotide exchange.
-
(1996)
Nature
, vol.379
, pp. 511-518
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-
Kawashima, T.1
Berthet-Colominas, C.2
Wulff, M.3
Cusack, S.4
Leberman, R.5
-
30
-
-
0028879495
-
Properties of isolated domains of the elongation factor Tu from Thermus thermophilus HB8
-
of special interest. The isolated domain 1 of EF-Tu binds GTP and GDP with about the same affinity. Interactions between domains 1 and 3 seem to be important for the stability of EF-Tu. A weak interaction between Tyr-tRNA and isolated domain 1 suggests that domain 1 provides part of the binding site for aa-tRNA.
-
Nock S, Grillenbeck N, Ahmadian MR, Ribeiro S, Kreutzer R, Sprinzl M. Properties of isolated domains of the elongation factor Tu from Thermus thermophilus HB8. of special interest Eur J Biochem. 234:1995;132-139 The isolated domain 1 of EF-Tu binds GTP and GDP with about the same affinity. Interactions between domains 1 and 3 seem to be important for the stability of EF-Tu. A weak interaction between Tyr-tRNA and isolated domain 1 suggests that domain 1 provides part of the binding site for aa-tRNA.
-
(1995)
Eur J Biochem
, vol.234
, pp. 132-139
-
-
Nock, S.1
Grillenbeck, N.2
Ahmadian, M.R.3
Ribeiro, S.4
Kreutzer, R.5
Sprinzl, M.6
-
31
-
-
0029798075
-
Structure and importance of the dimerization domain in elongation factor Ts from Thermus thermophilus
-
of special interest. EF-Ts from T. thermophilus forms a stable dimer in solution and the monomer is about half the size of the one from E. coli. The dimer in T. thermophilus thus resembles one monomer of E. coli EF-Ts.
-
Jiang Y, Nock S, Nesper M, Sprinzl M, Sigler PB. Structure and importance of the dimerization domain in elongation factor Ts from Thermus thermophilus. of special interest Biochemistry. 35:1996;10269-10278 EF-Ts from T. thermophilus forms a stable dimer in solution and the monomer is about half the size of the one from E. coli. The dimer in T. thermophilus thus resembles one monomer of E. coli EF-Ts.
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(1996)
Biochemistry
, vol.35
, pp. 10269-10278
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Jiang, Y.1
Nock, S.2
Nesper, M.3
Sprinzl, M.4
Sigler, P.B.5
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32
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0019872620
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Identification of a histidine residue near the aminoacyl transfer ribonucleic acid binding site of elongation factor Tu
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Duffy L, Gerber L, Johnson AE, Miller DL. Identification of a histidine residue near the aminoacyl transfer ribonucleic acid binding site of elongation factor Tu. Biochemistry. 20:1981;4663-4666.
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(1981)
Biochemistry
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Duffy, L.1
Gerber, L.2
Johnson, A.E.3
Miller, D.L.4
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33
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0029003880
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Purification of aminoacyl-tRNA by affinity chromatography on immobilized Thermus thermophilus EF-Tu·GTP
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Ribeiro S, Nock S, Sprinzl M. Purification of aminoacyl-tRNA by affinity chromatography on immobilized Thermus thermophilus EF-Tu·GTP. Anal Biochem. 228:1995;330-335.
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(1995)
Anal Biochem
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Ribeiro, S.1
Nock, S.2
Sprinzl, M.3
-
34
-
-
0029049551
-
Macromolecular arrangement in the aminoacyl-tRNA-elongation factor Tu·GTP ternary complex. A fluorescence energy transfer study
-
of special interest. This paper presents fluorescence studies that determine distances between tRNA and EF-Tu in the ternary complex that are in good agreement with those in the crystal structure.
-
Watson BS, Hazlett TL, Eccleston JF, Davis C, Jameson DM, Johnson AE. Macromolecular arrangement in the aminoacyl-tRNA-elongation factor Tu·GTP ternary complex. A fluorescence energy transfer study. of special interest Biochemistry. 34:1995;7904-7912 This paper presents fluorescence studies that determine distances between tRNA and EF-Tu in the ternary complex that are in good agreement with those in the crystal structure.
-
(1995)
Biochemistry
, vol.34
, pp. 7904-7912
-
-
Watson, B.S.1
Hazlett, T.L.2
Eccleston, J.F.3
Davis, C.4
Jameson, D.M.5
Johnson, A.E.6
-
35
-
-
0028966003
-
Defining a smaller RNA substrate for elongation factor Tu
-
of special interest. This paper defines an acceptor minihelix that binds as well as aa-tRNA to EF-Tu and that is in good agreement with the crystal structure.
-
Nazarenko IA, Uhlenbeck OC. Defining a smaller RNA substrate for elongation factor Tu. of special interest Biochemistry. 34:1995;2545-2552 This paper defines an acceptor minihelix that binds as well as aa-tRNA to EF-Tu and that is in good agreement with the crystal structure.
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(1995)
Biochemistry
, vol.34
, pp. 2545-2552
-
-
Nazarenko, I.A.1
Uhlenbeck, O.C.2
-
37
-
-
0029886448
-
Ala
-
of outstanding interest. A G3 - U70 base pair known to be an identity element for Ala-tRNA synthetase is shown to have influence on the RNA-helix geometry when compared with other base pairs.
-
Ala. of outstanding interest FEBS Lett. 385:1996;15-20 A G3 - U70 base pair known to be an identity element for Ala-tRNA synthetase is shown to have influence on the RNA-helix geometry when compared with other base pairs.
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(1996)
FEBS Lett
, vol.385
, pp. 15-20
-
-
Limmer, S.1
Reif, B.2
Ott, G.3
Arnold, L.4
Sprinzl, M.5
-
39
-
-
0029990096
-
Mutants of EF-Tu defective in binding aminoacyl-tRNA
-
of special interest. This paper presents substitutions of EF-Tu in domain 1 at the interface between domains 1 and 3 of the EF-Tu·GTP configuration. The results of this paper show that the formation of the ternary complex is sensitive to many different alterations in the domain 1/domain 3 interface of EF-Tu.
-
Abdulkarim F, Ehrenberg M, Hughes D. Mutants of EF-Tu defective in binding aminoacyl-tRNA. of special interest FEBS Lett. 382:1996;297-303 This paper presents substitutions of EF-Tu in domain 1 at the interface between domains 1 and 3 of the EF-Tu·GTP configuration. The results of this paper show that the formation of the ternary complex is sensitive to many different alterations in the domain 1/domain 3 interface of EF-Tu.
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(1996)
FEBS Lett
, vol.382
, pp. 297-303
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-
Abdulkarim, F.1
Ehrenberg, M.2
Hughes, D.3
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40
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0027980558
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The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution
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Czworkowski J, Wang J, Steitz TA, Moore PB. The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution. EMBO J. 13:1994;3661-3668.
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(1994)
EMBO J
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Czworkowski, J.1
Wang, J.2
Steitz, T.A.3
Moore, P.B.4
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41
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-
0030585061
-
The structure of elongation factor G in complex with GDP: Conformational flexibility and nucleotide exchange
-
of outstanding interest. This paper describes very interesting structural differences between EF-G·GDP and nucleotide-free EF-G.
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Al-Karadaghi S, Ævarsson A, Garber M, Zheltonosova J, Liljas A. The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange. of outstanding interest Structure. 4:1996;555-565 This paper describes very interesting structural differences between EF-G·GDP and nucleotide-free EF-G.
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(1996)
Structure
, vol.4
, pp. 555-565
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Al-Karadaghi, S.1
Ævarsson, A.2
Garber, M.3
Zheltonosova, J.4
Liljas, A.5
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42
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0028059544
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Three-dimensional structure of the ribosomal translocase: Elongation factor G from Thermus thermophilus
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Ævarsson A, Brazhnikov E, Garber M, Zheltonosova J, Chirgadze Y, Al-Karadaghi S, Svensson LA, Liljas A. Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus. EMBO J. 13:1994;3669-3677.
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(1994)
EMBO J
, vol.13
, pp. 3669-3677
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Ævarsson, A.1
Brazhnikov, E.2
Garber, M.3
Zheltonosova, J.4
Chirgadze, Y.5
Al-Karadaghi, S.6
Svensson, L.A.7
Liljas, A.8
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43
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0030091227
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Protein synthesis: Imprinting through molecular mimicry
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of special interest. A good review of the macromolecular mimicry between EF-G and the ternary complex of EF-Tu. The large conformational change of EF-G that is proposed to take place upon activation is most probably not needed for ribosome function.
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Liljas A. Protein synthesis: imprinting through molecular mimicry. of special interest Curr Biol. 6:1996;247-249 A good review of the macromolecular mimicry between EF-G and the ternary complex of EF-Tu. The large conformational change of EF-G that is proposed to take place upon activation is most probably not needed for ribosome function.
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(1996)
Curr Biol
, vol.6
, pp. 247-249
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Liljas, A.1
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44
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0029915322
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Structure of the ternary complex of EF-Tu: Macromolecular mimicry in translation
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Nyborg J, Nissen P, Kjeldgaard M, Thirup S, Polekhina G, Clark BFC, Reshetnikova L. Structure of the ternary complex of EF-Tu: macromolecular mimicry in translation. Trends Biochem Sci. 21:1996;81-82.
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(1996)
Trends Biochem Sci
, vol.21
, pp. 81-82
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Nyborg, J.1
Nissen, P.2
Kjeldgaard, M.3
Thirup, S.4
Polekhina, G.5
Clark, B.F.C.6
Reshetnikova, L.7
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45
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0029145925
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Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3
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of special interest. It is shown that eRF3 is a GTP-binding protein that greatly stimulates recognition of the stop codon by eRF1.
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Zhouravleva G, Frolova L, Le Goff X, Le Guellec R, Inge-Vechtomov S, Kisselev L, Philippe M. Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3. of special interest EMBO J. 14:1995;4065-4072 It is shown that eRF3 is a GTP-binding protein that greatly stimulates recognition of the stop codon by eRF1.
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(1995)
EMBO J
, vol.14
, pp. 4065-4072
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Zhouravleva, G.1
Frolova, L.2
Le Goff, X.3
Le Guellec, R.4
Inge-Vechtomov, S.5
Kisselev, L.6
Philippe, M.7
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46
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0029975504
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Conserved motifs in prokaryotic and eukaryotic polypeptide release factors: TRNA-protein mimicry hypothesis
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of outstanding interest. Sequence comparisons of release factors with the C-terminal part of EF-G indicate a tRNA-mimicking region of release factors that recognizes the stop codon.
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Ito K, Ebihara K, Uno M, Nakamura Y. Conserved motifs in prokaryotic and eukaryotic polypeptide release factors: tRNA-protein mimicry hypothesis. of outstanding interest Proc Natl Acad Sci USA. 93:1996;5443-5448 Sequence comparisons of release factors with the C-terminal part of EF-G indicate a tRNA-mimicking region of release factors that recognizes the stop codon.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 5443-5448
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Ito, K.1
Ebihara, K.2
Uno, M.3
Nakamura, Y.4
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47
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0026244229
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MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
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Kraulis PJ. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Cryst. 24:1991;946-950.
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(1991)
J Appl Cryst
, vol.24
, pp. 946-950
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Kraulis, P.J.1
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48
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84889120137
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Improved methods for building protein models in electron density maps and the location of errors in these models
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Jones TA, Cowan S, Zou J-Y, Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst A. 47:1991;110-119.
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(1991)
Acta Cryst a
, vol.47
, pp. 110-119
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Jones, T.A.1
Cowan, S.2
Zou, J.-Y.3
Kjeldgaard, M.4
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