-
1
-
-
0003110793
-
Factors involved in the transfer of aminoacyl-tRNA to the ribosome
-
H. Weissbach, Petska S. New York: Academic Press
-
Miller DL, Weissbach H. Factors involved in the transfer of aminoacyl-tRNA to the ribosome. Weissbach H, Petska S. Molecular Mechanisms of Protein Biosynthesis. 1977;323-373 Academic Press, New York.
-
(1977)
Molecular Mechanisms of Protein Biosynthesis
, pp. 323-373
-
-
Miller, D.L.1
Weissbach, H.2
-
2
-
-
0018089806
-
The role of guanosine 5-triphosphate in polypeptide elongation
-
Kaziro Y. The role of guanosine 5-triphosphate in polypeptide elongation. Biochem Biophys Acta. 505:1978;95-127.
-
(1978)
Biochem Biophys Acta
, vol.505
, pp. 95-127
-
-
Kaziro, Y.1
-
3
-
-
0029608909
-
Ribosomal proteins and elongation factors
-
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.
-
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.
-
(1995)
Curr Opin Struct Biol
, vol.5
, pp. 721-727
-
-
Liljas, A.1
Garber, M.2
-
4
-
-
0026026818
-
The GTPase superfamily: Conserved structure and molecular mechanisms
-
Bourne HR, Sanders DA, McCormick F. The GTPase superfamily: conserved structure and molecular mechanisms. Nature. 349:1991;117-127.
-
(1991)
Nature
, vol.349
, pp. 117-127
-
-
Bourne, H.R.1
Sanders, D.A.2
McCormick, F.3
-
5
-
-
0027394282
-
Structural aspects of ribonucleoprotein interactions in ribosomes
-
Yonath A, Franceschi F. Structural aspects of ribonucleoprotein interactions in ribosomes. Curr Opin Struct Biol. 3:1993;45-49.
-
(1993)
Curr Opin Struct Biol
, vol.3
, pp. 45-49
-
-
Yonath, A.1
Franceschi, F.2
-
6
-
-
0026588965
-
Refined structure of elongation factor EF-Tu from Escherichia coli
-
Kjeldgaard M, Nyborg J. Refined structure of elongation factor EF-Tu from Escherichia coli. J Mol Biol. 223:1992;721-742.
-
(1992)
J Mol Biol
, vol.223
, pp. 721-742
-
-
Kjeldgaard, M.1
Nyborg, J.2
-
7
-
-
0345482977
-
The GTP-binding domain: Three consensus sequences elements with distinct spacing
-
Dever TE, Glynias MJ, Merrick WC. The GTP-binding domain: three consensus sequences elements with distinct spacing. Proc Natl Acad Sci USA. 84:1987;1814-1818.
-
(1987)
Proc Natl Acad Sci USA
, vol.84
, pp. 1814-1818
-
-
Dever, T.E.1
Glynias, M.J.2
Merrick, W.C.3
-
8
-
-
0027179878
-
Crystal structure of active elongation factor Tu reveals major domain rearrangement
-
Berchtold H, Reshetnikova L, Reiser COA, Schirmer NK, Sprinzl M, Hilgenfeld R. Crystal structure of active elongation factor Tu reveals major domain rearrangement. Nature. 365:1993;126-132.
-
(1993)
Nature
, vol.365
, pp. 126-132
-
-
Berchtold, H.1
Reshetnikova, L.2
Reiser, C.O.A.3
Schirmer, N.K.4
Sprinzl, M.5
Hilgenfeld, R.6
-
9
-
-
0027917990
-
The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation
-
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.
-
(1993)
Structure
, vol.1
, pp. 35-50
-
-
Kjeldgaard, M.1
Nissen, P.2
Thirup, S.3
Nyborg, J.4
-
10
-
-
0028871610
-
Interaction of guanosine nucleotides and their analogs with elongation factor Tu from Thermus thermophilus
-
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.
-
(1995)
Biochemistry
, vol.34
, pp. 12535-12542
-
-
Wagner, A.1
Simon, I.2
Sprinzl, M.3
Goody, R.S.4
-
11
-
-
0028819527
-
Mutation of the conserved Gly94 and Gly126 in elongation factor Tu from Escherichia coli. Elucidation of their structural and functional roles
-
Knudsen CR, Kjærsgaard IV, Wiborg O, Clark BFC. Mutation of the conserved Gly94 and Gly126 in elongation factor Tu from Escherichia coli. Elucidation of their structural and functional roles. Eur J Biochem. 228:1995;176-183.
-
(1995)
Eur J Biochem
, vol.228
, pp. 176-183
-
-
Knudsen, C.R.1
Kjærsgaard, I.V.2
Wiborg, O.3
Clark, B.F.C.4
-
12
-
-
0028895690
-
Mutation of the conserved Gly83 and Gly94 in Escherichia coli elongation factor Tu. Indication of structural pivots
-
of special interest. The two glycine residues found at the amino and carboxyl termini of helix B in EF-Tu·GDP are important for the large rearrangement of domains upon activation of EF-Tu.
-
Kjærsgaard IV, Knudsen CR, Wiborg O. Mutation of the conserved Gly83 and Gly94 in Escherichia coli elongation factor Tu. Indication of structural pivots. of special interest Eur J Biochem. 228:1995;184-190 The two glycine residues found at the amino and carboxyl termini of helix B in EF-Tu·GDP are important for the large rearrangement of domains upon activation of EF-Tu.
-
(1995)
Eur J Biochem
, vol.228
, pp. 184-190
-
-
Kjærsgaard, I.V.1
Knudsen, C.R.2
Wiborg, O.3
-
13
-
-
0027980558
-
The crystal structure of elongation factor G complexed with GDP, at 2,7 Å resolution
-
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.
-
(1994)
EMBO J
, vol.13
, pp. 3661-3668
-
-
Czworkowski, J.1
Wang, J.2
Steitz, T.A.3
Moore, P.B.4
-
14
-
-
0028059544
-
Three-dimensional structure of the ribosomal translocase: Elongation factor G from Thermus thermophilus
-
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.
-
(1994)
EMBO J
, vol.13
, pp. 3669-3677
-
-
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
-
15
-
-
0028774177
-
The ABC of EF-G
-
Jurnak J. The ABC of EF-G. Structure. 2:1994;785-788.
-
(1994)
Structure
, vol.2
, pp. 785-788
-
-
Jurnak, J.1
-
16
-
-
0029182369
-
A ribosomal protein module in EF-G and DNA gyrase
-
Murzin AG. A ribosomal protein module in EF-G and DNA gyrase. Nat Struct Biol. 2:1995;25-26.
-
(1995)
Nat Struct Biol
, vol.2
, pp. 25-26
-
-
Murzin, A.G.1
-
17
-
-
0028812785
-
Phe, EF-Tu, and a GTP analog
-
of outstanding interest. The first cyrstal structure of the ternary complex of EF-Tu reveals details of the tRNA binding that are different from what was expected from many biochemical results. The unexpected similarity to 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.
-
Phe, EF-Tu, and a GTP analog. of outstanding interest Science. 270:1995;1464-1472 The first cyrstal structure of the ternary complex of EF-Tu reveals details of the tRNA binding that are different from what was expected from many biochemical results. The unexpected similarity to 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.
-
(1995)
Science
, vol.270
, pp. 1464-1472
-
-
Nissen, P.1
Kjeldgaard, M.2
Thirup, S.3
Polekhina, G.4
Reshetnikova, L.5
Clark, B.F.C.6
Nyborg, J.7
-
18
-
-
0019872620
-
Identification of a histidine residue near the aminoacyl transfer ribonucleic acid binding site of elongation factor Tu
-
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.
-
(1981)
Biochemistry
, vol.20
, pp. 4663-4666
-
-
Duffy, L.1
Gerber, L.2
Johnson, A.E.3
Miller, D.L.4
-
19
-
-
0029049551
-
Macromolecular arrangement in the aminoacyl-tRNA-delongation factor Tu-GTP ternary complex. A fluorescence energy transfer study
-
of special interest. These studies give distances between the tRNA EF-Tu in good agreement with the crystal structure.
-
Watson BS, Hazlett TL, Eccleston JF, Davis C, Jameson DM, Johnson AE. Macromolecular arrangement in the aminoacyl-tRNA-delongation factor Tu-GTP ternary complex. A fluorescence energy transfer study. of special interest Biochemistry. 34:1995;7904-7912 These studies give distances between the tRNA EF-Tu in good agreement with 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
-
20
-
-
0028966003
-
Defining a smaller RNA substrate for elongation factor Tu
-
of special interest. The definition of an acceptor mini helix that binds to aa-tRNA as well as to EF-Tu 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 The definition of an acceptor mini helix that binds to aa-tRNA as well as to EF-Tu is in good agreement with the crystal structure.
-
(1995)
Biochemistry
, vol.34
, pp. 2545-2552
-
-
Nazarenko, I.A.1
Uhlenbeck, O.C.2
-
21
-
-
0029002506
-
Phosphorylation of elongation factor Tu prevents ternary complex formation
-
Alexander C, Bilgin N, Lindschau C, Mesters JR, Kraal B, Hilgenfeld R, Erdmann VA, Lippmann C. Phosphorylation of elongation factor Tu prevents ternary complex formation. J Biol Chem. 270:1995;14541-14547.
-
(1995)
J Biol Chem
, vol.270
, pp. 14541-14547
-
-
Alexander, C.1
Bilgin, N.2
Lindschau, C.3
Mesters, J.R.4
Kraal, B.5
Hilgenfeld, R.6
Erdmann, V.A.7
Lippmann, C.8
-
22
-
-
0027418991
-
Toward a model for the interaction between elongation factor Tu and the ribosome
-
Weijland A, Parmeggiani A. Toward a model for the interaction between elongation factor Tu and the ribosome. Science. 259:1993;1311-1314.
-
(1993)
Science
, vol.259
, pp. 1311-1314
-
-
Weijland, A.1
Parmeggiani, A.2
-
23
-
-
0028960178
-
Switching nucleotide specificity of Ha-ras p21 by a single amino acid substitution at aspartate 119
-
Zhong JM, Chen-Hwang MC, Hwang YW. Switching nucleotide specificity of Ha-ras p21 by a single amino acid substitution at aspartate 119. J Biol Chem. 270:1995;10002-10007.
-
(1995)
J Biol Chem
, vol.270
, pp. 10002-10007
-
-
Zhong, J.M.1
Chen-Hwang, M.C.2
Hwang, Y.W.3
-
24
-
-
0028351548
-
Two GTPs are hydrolysed on two molecules of EF-Tu for each elongation cycle during code translation
-
Scoble J, Bilgin N, Ehrenberg M. Two GTPs are hydrolysed on two molecules of EF-Tu for each elongation cycle during code translation. Biochimie. 76:1994;59-62.
-
(1994)
Biochimie
, vol.76
, pp. 59-62
-
-
Scoble, J.1
Bilgin, N.2
Ehrenberg, M.3
-
25
-
-
0028934880
-
Stoichiometry for the elongation factor Tu-aminoacyl-tRNA complex switches with temperature
-
Bilgin N, Ehrenberg M. Stoichiometry for the elongation factor Tu-aminoacyl-tRNA complex switches with temperature. Biochemistry. 34:1995;715-719.
-
(1995)
Biochemistry
, vol.34
, pp. 715-719
-
-
Bilgin, N.1
Ehrenberg, M.2
-
26
-
-
0028848882
-
Two GTPs are consumed on EF-Tu per peptide bond in poly(Phe) synthesis, in spite of switching stoichiometry of the EF-Tu·aminoacyl-tRNA complex with temperature
-
Dinçbas V, Bilgin N, Scoble J, Ehrenberg M. Two GTPs are consumed on EF-Tu per peptide bond in poly(Phe) synthesis, in spite of switching stoichiometry of the EF-Tu·aminoacyl-tRNA complex with temperature. FEBS Lett. 357:1995;19-22.
-
(1995)
FEBS Lett
, vol.357
, pp. 19-22
-
-
Dinçbas, V.1
Bilgin, N.2
Scoble, J.3
Ehrenberg, M.4
-
27
-
-
0028985402
-
Stoichiometry of the EF-Tu·GTP complex with aminoacyl-tRNA: Ternary quinternary?
-
Leberman R. Stoichiometry of the EF-Tu·GTP complex with aminoacyl-tRNA: ternary quinternary? FEBS Lett. 358:1995;71-72.
-
(1995)
FEBS Lett
, vol.358
, pp. 71-72
-
-
Leberman, R.1
-
28
-
-
0028941626
-
GTP consumption of elongation factor Tu during translation of heteropolymeric mRNAS
-
Rodnina MV, Wintermeyer W. GTP consumption of elongation factor Tu during translation of heteropolymeric mRNAS. Proc Natl Acad Sci USA. 92:1995;1945-1949.
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 1945-1949
-
-
Rodnina, M.V.1
Wintermeyer, W.2
-
29
-
-
0024458904
-
Intermediate states in the movement of transfer RNA in the ribosome
-
Moazed D, Noller HF. Intermediate states in the movement of transfer RNA in the ribosome. Nature. 342:1989;142-148.
-
(1989)
Nature
, vol.342
, pp. 142-148
-
-
Moazed, D.1
Noller, H.F.2
-
30
-
-
0030091227
-
Protein synthesis: Imprinting through molecular mimicry
-
of special interest. A good review on the macromolecular mimicry betwee EF·G and the ternary complex of EF-Tu. The large conformational change of EF·G upon activation proposed here is most probably not needed for ribosome function.
-
Liljas A. Protein synthesis: imprinting through molecular mimicry. of special interest Curr Biol. 6:1996;247-249 A good review on the macromolecular mimicry betwee EF·G and the ternary complex of EF-Tu. The large conformational change of EF·G upon activation proposed here is most probably not needed for ribosome function.
-
(1996)
Curr Biol
, vol.6
, pp. 247-249
-
-
Liljas, A.1
-
31
-
-
0030025671
-
The structure of the Escherichia coli EF-Tu:EF-Ts complex at 2.5 Å resolution
-
of outstanding interest. This structure 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 enable 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 This structure 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 enable nucleotide exchange.
-
(1996)
Nature
, vol.379
, pp. 511-518
-
-
Kawashima, T.1
Berthet-Colominas, C.2
Wulff, M.3
Cusack, S.4
Leberman, R.5
-
32
-
-
0029065576
-
Analysis and crystallization of a 25kDA C-terminal fragment of cloned elongation factor Ts from Escherichia coli
-
of special interest. It is shown that a 5 kDa amino-terminal domain is important for nucleotide exchange.
-
Bøgestrand S, Wiborg O, Thirup S, Nyborg J. Analysis and crystallization of a 25kDA C-terminal fragment of cloned elongation factor Ts from Escherichia coli. of special interest FEBS Lett. 368:1995;49-54 It is shown that a 5 kDa amino-terminal domain is important for nucleotide exchange.
-
(1995)
FEBS Lett
, vol.368
, pp. 49-54
-
-
Bøgestrand, S.1
Wiborg, O.2
Thirup, S.3
Nyborg, J.4
-
33
-
-
0024312593
-
Structure - Function relationships of elongation factor Tu. Isolation and activity of the guanine-nucleotide-binding domain
-
Jensen M, Cool RH, Mortensen KK, Clark BFC, Parmeggiani A. Structure - function relationships of elongation factor Tu. Isolation and activity of the guanine-nucleotide-binding domain. Eur J Biochem. 182:1989;247-255.
-
(1989)
Eur J Biochem
, vol.182
, pp. 247-255
-
-
Jensen, M.1
Cool, R.H.2
Mortensen, K.K.3
Clark, B.F.C.4
Parmeggiani, A.5
-
34
-
-
0029100747
-
A model of protein synthesis based on a new cryo-electron microscopy reconstruction of the E. coli ribosome
-
of outstanding interest. The most detailed structural model from cryo-EM presented so far. Several new channels are seen in this model.
-
Frank J, Zhu J, Penczek P, Li Y, Srivastava S, Veshoor A, Radermarcher 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 from cryo-EM presented so far. Several new channels are seen in this model.
-
(1995)
Nature
, vol.376
, pp. 441-444
-
-
Frank, J.1
Zhu, J.2
Penczek, P.3
Li, Y.4
Srivastava, S.5
Veshoor, A.6
Radermarcher, M.7
Grassucci, R.8
Lata, R.K.9
Agrawal, R.K.10
-
35
-
-
0029645318
-
The 70S Escherichia coli ribosome at 23 Å resolution: Fitting the ribosomal RNA
-
of outstanding interest. Another reconstruction from cryo-EM very similar to the previous reference [34]. Some helical sections of rRNA are fitted into the model.
-
Stark H, Mÿller 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 reconstruction from cryo-EM very similar to the previous reference [34]. Some helical sections of rRNA are fitted into the model.
-
(1995)
Structure
, vol.3
, pp. 815-821
-
-
Stark, H.1
Mÿller, 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
-
36
-
-
0029044829
-
The structure of ribosomal RNA: A three-dimensional jigsaw puzzle
-
of special interest. A comprehensive collection of biochemical and structural data is used to propose a model for rRNA.
-
Brimacombe R. The structure of ribosomal RNA: a three-dimensional jigsaw puzzle. of special interest Eur J Biochem. 230:1995;365-383 A comprehensive collection of biochemical and structural data is used to propose a model for rRNA.
-
(1995)
Eur J Biochem
, vol.230
, pp. 365-383
-
-
Brimacombe, R.1
-
37
-
-
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 ends. 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 ends. The angle between the planes of these two tRNAs is larger than expected.
-
(1996)
Science
, vol.271
, pp. 1000-1002
-
-
Agrawal, R.K.1
Penczek, P.2
Grassucci, R.A.3
Li, Y.4
Leith, A.5
Nierhaus, K.H.6
Frank, J.7
-
38
-
-
0029006133
-
Condon-dependent conformational change of elongation factor Tu preceding GTP hydrolysis on the ribosome
-
Rodnina MV, Fricke R, Kuhn L, Wintermeyer W. Condon-dependent conformational change of elongation factor Tu preceding GTP hydrolysis on the ribosome. EMBO J. 14:1995;2613-2619.
-
(1995)
EMBO J
, vol.14
, pp. 2613-2619
-
-
Rodnina, M.V.1
Fricke, R.2
Kuhn, L.3
Wintermeyer, W.4
-
39
-
-
0028923491
-
How do the GTPases really work?
-
Hilgenfeld R. How do the GTPases really work? Nat Struct Biol. 2:1995;3-6.
-
(1995)
Nat Struct Biol
, vol.2
, pp. 3-6
-
-
Hilgenfeld, R.1
-
40
-
-
0029559655
-
Regulatory GTPases
-
of special interest. A nice review on the structures of GTPases.
-
Hilgenfeld R. Regulatory GTPases. of special interest Curr Opin Struct Biol. 5:1995;810-817 A nice review on the structures of GTPases.
-
(1995)
Curr Opin Struct Biol
, vol.5
, pp. 810-817
-
-
Hilgenfeld, R.1
-
44
-
-
0029061952
-
Relevance of histidine-84 in the elongation factor Tu GTPase activity and in poly(Phe) synthesis: Its substitution by glutamine and alanine
-
Scarano G, Krab IM, Bocchini V, Parmeggiani A. Relevance of histidine-84 in the elongation factor Tu GTPase activity and in poly(Phe) synthesis: its substitution by glutamine and alanine. FEBS Lett. 365:1995;214-218.
-
(1995)
FEBS Lett
, vol.365
, pp. 214-218
-
-
Scarano, G.1
Krab, I.M.2
Bocchini, V.3
Parmeggiani, A.4
-
45
-
-
0028937947
-
Site-directed mutagenesis of Thermus thermophilus elongation factor Tu. Replacement of His85, Asp81 and Arg300
-
Zeidler W, Egle C, Ribeiro S, Wagner A, Katunin V, Kreutzer R, Rodnina M, Wintermeyer W, Sprinzl M. Site-directed mutagenesis of Thermus thermophilus elongation factor Tu. Replacement of His85, Asp81 and Arg300. Eur J Biochem. 229:1995;596-604.
-
(1995)
Eur J Biochem
, vol.229
, pp. 596-604
-
-
Zeidler, W.1
Egle, C.2
Ribeiro, S.3
Wagner, A.4
Katunin, V.5
Kreutzer, R.6
Rodnina, M.7
Wintermeyer, W.8
Sprinzl, M.9
-
46
-
-
0029548957
-
Site-directed mutagenesis of Arg48 and Asp86 of elongation factor Tu from Escherichia coli: Effects on the GTPase reaction and aminoacyl-tRNA binding
-
of special interest. Residue Arg58 is shown to be of little importance for intrinsic GTP hydrolysis but to have some influence on the ribosome-stimulated GTPase activity.
-
Knudsen CR, Clark BFC. Site-directed mutagenesis of Arg48 and Asp86 of elongation factor Tu from Escherichia coli: effects on the GTPase reaction and aminoacyl-tRNA binding. of special interest Protein Eng. 8:1995;1267-1273 Residue Arg58 is shown to be of little importance for intrinsic GTP hydrolysis but to have some influence on the ribosome-stimulated GTPase activity.
-
(1995)
Protein Eng
, vol.8
, pp. 1267-1273
-
-
Knudsen, C.R.1
Clark, B.F.C.2
-
47
-
-
0026244229
-
MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
-
Kraulis PJ. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr. 24:1991;946-950.
-
(1991)
J Appl Crystallogr
, vol.24
, pp. 946-950
-
-
Kraulis, P.J.1
-
48
-
-
84889120137
-
Improved methods for building protein models in electron density maps and the location of errors in these models
-
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 Crystallogr A - Found Crystallogr. 47:1991;110-119.
-
(1991)
Acta Crystallogr A - Found Crystallogr
, vol.47
, pp. 110-119
-
-
Jones, T.A.1
Cowan, S.2
Zou J-Y3
Kjeldgaard, M.4
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