메뉴 건너뛰기




Volumn 105, Issue 2, 2008, Pages 500-505

Cross-crystal averaging reveals that the structure of the peptidyl-transferase center is the same in the 70S ribosome and the 50S subunit

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDYLTRANSFERASE;

EID: 38649126163     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0711076105     Document Type: Article
Times cited : (17)

References (34)
  • 1
    • 0034699518 scopus 로고    scopus 로고
    • Structure of the 30S ribosomal subunit
    • Wimberly BT, et al. (2000) Structure of the 30S ribosomal subunit. Nature 407:327-339.
    • (2000) Nature , vol.407 , pp. 327-339
    • Wimberly, B.T.1
  • 2
    • 0034699519 scopus 로고    scopus 로고
    • Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics
    • Carter AP, et al. (2000) Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics. Nature 407:340-348.
    • (2000) Nature , vol.407 , pp. 340-348
    • Carter, A.P.1
  • 3
    • 0035805229 scopus 로고    scopus 로고
    • Recognition of cognate transfer RNA by the 30S ribosomal subunit
    • Ogle JM, et al. (2001) Recognition of cognate transfer RNA by the 30S ribosomal subunit. Science 292:897-902.
    • (2001) Science , vol.292 , pp. 897-902
    • Ogle, J.M.1
  • 4
    • 0037184536 scopus 로고    scopus 로고
    • Selection of tRNA by the ribosome requires a transition from an open to a closed form
    • Ogle JM, Murphy FV, Tarry MJ, Ramakrishnan V (2002) Selection of tRNA by the ribosome requires a transition from an open to a closed form. Cell 111:721-732.
    • (2002) Cell , vol.111 , pp. 721-732
    • Ogle, J.M.1    Murphy, F.V.2    Tarry, M.J.3    Ramakrishnan, V.4
  • 5
    • 0034637161 scopus 로고    scopus 로고
    • The structural basis of ribosome activity in peptide bond synthesis
    • Nissen P, Hansen J, Ban N, Moore PB, Steitz TA (2000) The structural basis of ribosome activity in peptide bond synthesis. Science 289:920-930.
    • (2000) Science , vol.289 , pp. 920-930
    • Nissen, P.1    Hansen, J.2    Ban, N.3    Moore, P.B.4    Steitz, T.A.5
  • 6
    • 0036177483 scopus 로고    scopus 로고
    • A pre-translocational intermediate in protein synthesis observed in crystals of enzymatically active 50S subunits
    • Schmeing TM, et al. (2002) A pre-translocational intermediate in protein synthesis observed in crystals of enzymatically active 50S subunits. Nat Struct Biol 9:225-230.
    • (2002) Nat Struct Biol , vol.9 , pp. 225-230
    • Schmeing, T.M.1
  • 7
    • 0142178293 scopus 로고    scopus 로고
    • Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit
    • Schmeing TM, Moore PB, Steitz TA (2003) Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit. RNA 9:1345-1352.
    • (2003) RNA , vol.9 , pp. 1345-1352
    • Schmeing, T.M.1    Moore, P.B.2    Steitz, T.A.3
  • 8
    • 27644557445 scopus 로고    scopus 로고
    • Structural insights into the roles of water and the 2′ hydroxyl of the P site tRNA in the peptidyl transferase reaction
    • Schmeing TM, Huang KS, Kitchen DE, Strobel SA, Steitz TA (2005) Structural insights into the roles of water and the 2′ hydroxyl of the P site tRNA in the peptidyl transferase reaction. Mol Cell 20:437-448.
    • (2005) Mol Cell , vol.20 , pp. 437-448
    • Schmeing, T.M.1    Huang, K.S.2    Kitchen, D.E.3    Strobel, S.A.4    Steitz, T.A.5
  • 9
    • 28544452248 scopus 로고    scopus 로고
    • An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA
    • Schmeing TM, Huang KS, Strobel SA, Steitz TA (2005) An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA. Nature 438:520-524.
    • (2005) Nature , vol.438 , pp. 520-524
    • Schmeing, T.M.1    Huang, K.S.2    Strobel, S.A.3    Steitz, T.A.4
  • 10
    • 0033592361 scopus 로고    scopus 로고
    • A possible mechanism of peptide bond formation on ribosome without mediation of peptidyl transferase
    • Das GK, Bhattacharyya D, Burma DP (1999) A possible mechanism of peptide bond formation on ribosome without mediation of peptidyl transferase. J Theor Biol 200:193-205.
    • (1999) J Theor Biol , vol.200 , pp. 193-205
    • Das, G.K.1    Bhattacharyya, D.2    Burma, D.P.3
  • 11
    • 0037069377 scopus 로고    scopus 로고
    • Catalysis of amide synthesis by RNA phosphodiester and hydroxyl groups
    • Chamberlin SI, Merino EJ, Weeks KM (2002) Catalysis of amide synthesis by RNA phosphodiester and hydroxyl groups. Proc Natl Acad Sci USA 99:14688-14693.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14688-14693
    • Chamberlin, S.I.1    Merino, E.J.2    Weeks, K.M.3
  • 13
    • 0345099498 scopus 로고    scopus 로고
    • Mononucleotide derivatives as ribosomal P-site substrates reveal an important contribution of the 2′-OH to activity
    • Dorner S, Panuschka C, Schmid W, Barta A (2003) Mononucleotide derivatives as ribosomal P-site substrates reveal an important contribution of the 2′-OH to activity. Nucleic Acids Res 31:6536-6542.
    • (2003) Nucleic Acids Res , vol.31 , pp. 6536-6542
    • Dorner, S.1    Panuschka, C.2    Schmid, W.3    Barta, A.4
  • 15
    • 23944472625 scopus 로고    scopus 로고
    • What are the roles of substrate-assisted catalysis and proximity effects in peptide bond formation by the ribosome?
    • Sharma PK, Xiang Y, Kato M, Warshel A (2005) What are the roles of substrate-assisted catalysis and proximity effects in peptide bond formation by the ribosome? Biochemistry 44:11307-11314.
    • (2005) Biochemistry , vol.44 , pp. 11307-11314
    • Sharma, P.K.1    Xiang, Y.2    Kato, M.3    Warshel, A.4
  • 16
    • 24644461086 scopus 로고    scopus 로고
    • Mechanism of peptide bond synthesis on the ribosome
    • Trobro S, Aqvist J (2005) Mechanism of peptide bond synthesis on the ribosome. Proc Natl Acad Sci USA 102:12395-12400.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 12395-12400
    • Trobro, S.1    Aqvist, J.2
  • 17
    • 33745048734 scopus 로고    scopus 로고
    • Analysis of predictions for the catalytic mechanism of ribosomal peptidyl transfer
    • Trobro S, Aqvist J (2006) Analysis of predictions for the catalytic mechanism of ribosomal peptidyl transfer. Biochemistry 45:7049-7056.
    • (2006) Biochemistry , vol.45 , pp. 7049-7056
    • Trobro, S.1    Aqvist, J.2
  • 18
    • 33646141185 scopus 로고    scopus 로고
    • The syn-oriented 2′-OH provides a favorable proton transfer geometry in 1,2-diol monoester aminolysis: Implications for the ribosome mechanism
    • Rangelov MA, Vayssilov GN, Yomtova VM, Petkov DD (2006) The syn-oriented 2′-OH provides a favorable proton transfer geometry in 1,2-diol monoester aminolysis: Implications for the ribosome mechanism. J Am Chem Soc 128:4964-4965.
    • (2006) J Am Chem Soc , vol.128 , pp. 4964-4965
    • Rangelov, M.A.1    Vayssilov, G.N.2    Yomtova, V.M.3    Petkov, D.D.4
  • 20
    • 33749354360 scopus 로고    scopus 로고
    • Structure of the 70S ribosome complexed with mRNA and tRNA
    • Selmer M, et al. (2006) Structure of the 70S ribosome complexed with mRNA and tRNA. Science 313:1935-1942.
    • (2006) Science , vol.313 , pp. 1935-1942
    • Selmer, M.1
  • 21
    • 33748582906 scopus 로고    scopus 로고
    • Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements
    • Korostelev A, Trakhanov S, Laurberg M, Noller HF (2006) Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements. Cell 126:1065-1077.
    • (2006) Cell , vol.126 , pp. 1065-1077
    • Korostelev, A.1    Trakhanov, S.2    Laurberg, M.3    Noller, H.F.4
  • 22
    • 0033198415 scopus 로고    scopus 로고
    • Error estimation and bias correction in phase-improvement calculations
    • Cowtan K (1999) Error estimation and bias correction in phase-improvement calculations. Acta Crystallogr D 55:1555-1567.
    • (1999) Acta Crystallogr D , vol.55 , pp. 1555-1567
    • Cowtan, K.1
  • 23
    • 0033813066 scopus 로고    scopus 로고
    • Ternary complex between placental lactogen and the extracellular domain of the prolactin receptor
    • Elkins PA, et al. (2000) Ternary complex between placental lactogen and the extracellular domain of the prolactin receptor. Nat Struct Biol 7:808-815.
    • (2000) Nat Struct Biol , vol.7 , pp. 808-815
    • Elkins, P.A.1
  • 24
    • 0035902009 scopus 로고    scopus 로고
    • Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors
    • Brejc K, et al. (2001) Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors. Nature 411:269-276.
    • (2001) Nature , vol.411 , pp. 269-276
    • Brejc, K.1
  • 26
    • 34147098650 scopus 로고    scopus 로고
    • The crystal structure of yeast fatty acid synthase, a cellular machine with eight active sites working together
    • Lomakin IB, Xiong Y, Steitz TA (2007) The crystal structure of yeast fatty acid synthase, a cellular machine with eight active sites working together. Cell 129:319-332.
    • (2007) Cell , vol.129 , pp. 319-332
    • Lomakin, I.B.1    Xiong, Y.2    Steitz, T.A.3
  • 27
    • 16644372753 scopus 로고    scopus 로고
    • Atomic model of the Thermus thermophilus 70S ribosome developed in silico
    • Tung CS, Sanbonmatsu KY (2004) Atomic model of the Thermus thermophilus 70S ribosome developed in silico. Biophys J 87:2714-2722.
    • (2004) Biophys J , vol.87 , pp. 2714-2722
    • Tung, C.S.1    Sanbonmatsu, K.Y.2
  • 28
    • 0035805213 scopus 로고    scopus 로고
    • Crystal structure of the ribosome at 5.5 Å resolution
    • Yusupov MM, et al. (2001) Crystal structure of the ribosome at 5.5 Å resolution. Science 292:883-896.
    • (2001) Science , vol.292 , pp. 883-896
    • Yusupov, M.M.1
  • 29
    • 27644491082 scopus 로고    scopus 로고
    • Structures of the bacterial ribosome at 3.5 Å resolution
    • Schuwirth BS, et al. (2005) Structures of the bacterial ribosome at 3.5 Å resolution. Science 310:827-834.
    • (2005) Science , vol.310 , pp. 827-834
    • Schuwirth, B.S.1
  • 30
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D 53:240-255.
    • (1997) Acta Crystallogr D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 31
    • 0033119386 scopus 로고    scopus 로고
    • Software for handling macromolecular envelopes
    • Kleywegt GJ, Jones TA (1999) Software for handling macromolecular envelopes. Acta Crystallogr D 55:941-944.
    • (1999) Acta Crystallogr D , vol.55 , pp. 941-944
    • Kleywegt, G.J.1    Jones, T.A.2
  • 32
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D 60:2126-2132.
    • (2004) Acta Crystallogr D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 33
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47:110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 34
    • 0032872798 scopus 로고    scopus 로고
    • Density modification for macromolecular phase improvement
    • Cowtan KD, Zhang KY (1999) Density modification for macromolecular phase improvement. Prog Biophys Mol Biol 72:245-270.
    • (1999) Prog Biophys Mol Biol , vol.72 , pp. 245-270
    • Cowtan, K.D.1    Zhang, K.Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.