Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression (559 views)
Mol Cell (ISSN: 1097-2765, 1097-4164), 2003 Jan; 11(1): 91-102.
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Paper type: Journal Article,
Impact factor: 16.835, 5-year impact factor: 15.324
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0037249473&partnerID=40&md5=52d8a5e881217cbef1352eca066e6a15
Keywords: Peptidyltransferase, Puromycin, Ribosome Rna, Transfer Rna, Article, Chemical Bond, Chemical Interaction, Conformational Transition, Crystal Structure, Deinococcus Radiodurans, Nonhuman, Protein Conformation, Ribosome Subunit, Rna Structure, Rna Transport, Bacterial Proteins, Catalytic Domain, Crystallography, X-Ray, Models, Molecular, Molecular Structure, Nucleic Acid Conformation, Protein Biosynthesis, Protein Synthesis Inhibitors, Ribosomal Proteins, Amino Acyl, Sparsomycin,
Affiliations:
*** IBB - CNR ***
Department of Structural Biology, Weizmann Institute, 76100 Rehovot, Israel
Max-Planck-Res. U. for Ribosomal S., Notkestrasse 85, 22603 Hamburg, Germany
FB Biologie, Chemie, Pharmazie, Frei University Berlin, Takustrasse 3, 14195 Berlin, Germany
Inst. of Biostructures and Bioimages, CNR, 80138 Napoli, Italy
References:
Not available.
Mol Cell (ISSN: 1097-2765, 1097-4164), 2003 Jan; 11(1): 91-102.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 16.835, 5-year impact factor: 15.324
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0037249473&partnerID=40&md5=52d8a5e881217cbef1352eca066e6a15
Keywords: Peptidyltransferase, Puromycin, Ribosome Rna, Transfer Rna, Article, Chemical Bond, Chemical Interaction, Conformational Transition, Crystal Structure, Deinococcus Radiodurans, Nonhuman, Protein Conformation, Ribosome Subunit, Rna Structure, Rna Transport, Bacterial Proteins, Catalytic Domain, Crystallography, X-Ray, Models, Molecular, Molecular Structure, Nucleic Acid Conformation, Protein Biosynthesis, Protein Synthesis Inhibitors, Ribosomal Proteins, Amino Acyl, Sparsomycin,
Affiliations:
*** IBB - CNR ***
Department of Structural Biology, Weizmann Institute, 76100 Rehovot, Israel
Max-Planck-Res. U. for Ribosomal S., Notkestrasse 85, 22603 Hamburg, Germany
FB Biologie, Chemie, Pharmazie, Frei University Berlin, Takustrasse 3, 14195 Berlin, Germany
Inst. of Biostructures and Bioimages, CNR, 80138 Napoli, Italy
References:
Not available.
Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression
Crystal structures of tRNA mimics complexed with the large ribosomal subunit of Deinococcus radiodurans indicate that remote interactions determine the precise orientation of tRNA in the peptidyl-transferase center (PTC). The PTC tolerates various orientations of puromycin derivatives and its flexibility allows the conformational rearrangements required for peptide-bond formation. Sparsomycin binds to A2602 and alters the PTC conformation. H69, the intersubunit-bridge connecting the PTC and decoding site, may also participate in tRNA placement and translocation. A spiral rotation of the 3′ end of the A-site tRNA around a 2-fold axis of symmetry identified within the PTC suggests a unified ribosomal machinery for peptide-bond formation, A-to-P-site translocation, and entrance of nascent proteins into the exit tunnel. Similar 2-fold related regions, detected in all known structures of large ribosomal subunits, indicate the universality of this mechanism.
Crystal structures of tRNA mimics complexed with the large ribosomal subunit of Deinococcus radiodurans indicate that remote interactions determine the precise orientation of tRNA in the peptidyl-transferase center (PTC). The PTC tolerates various orientations of puromycin derivatives and its flexibility allows the conformational rearrangements required for peptide-bond formation. Sparsomycin binds to A2602 and alters the PTC conformation. H69, the intersubunit-bridge connecting the PTC and decoding site, may also participate in tRNA placement and translocation. A spiral rotation of the 3′ end of the A-site tRNA around a 2-fold axis of symmetry identified within the PTC suggests a unified ribosomal machinery for peptide-bond formation, A-to-P-site translocation, and entrance of nascent proteins into the exit tunnel. Similar 2-fold related regions, detected in all known structures of large ribosomal subunits, indicate the universality of this mechanism.
Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression
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Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression
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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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Impact Factor: 3.843
View Export to BibTeX Export to EndNote
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Impact Factor: 2.438
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Bashan A, Zarivach R, Schluenzen F, Agmon I, Harms J, Auerbach T, Baram D, Berisio R, Bartels H, Hansen HAS, Fucini P, Wilson D, Peretz M, Kessler M, Yonath A
* Ribosomal crystallography: Peptide bond formation and its inhibition (654 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2003 Sep; 70(1): 19-41.
Impact Factor: 2.733
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Berisio R, Schluenzen F, Harms J, Bashan A, Auerbach T, Baram D, Yonath A
* Structural insight into the role of the ribosomal tunnel in cellular regulation (519 views)
Nat Struct Biol (ISSN: 1072-8368), 2003 May; 10(5): 366-370.
Impact Factor: 11.579
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Bonomo RP, Bruno V, Conte E, De Guidi G, La Mendola D, Maccarrone G, Nicoletti F, Rizzarelli E, Sortino S, Vecchio G
* Potentiometric, spectroscopic and antioxidant activity studies of SOD mimics containing carnosine (451 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2003; (23): 4406-4415.
Impact Factor: 2.908
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Menziani MC, De Benedetti PG, Langella E, Barone V
* Seeking for binding determinants of the prion protein to human plasminogen (538 views)
Mol Phys (ISSN: 0026-8976), 2003; 101(17): 2763-2773.
Impact Factor: 1.591
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Masullo M, Cantiello P, Paola B, Fiengo A, Vitagliano L, Zagari A, Arcari P
* Valine114 Replacements In The Archaeal Elongation Factor 1a Enhanced Its Ability To Interact With Aminoacyl-Trna And Kirromycin (452 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2002; 41(49): 14482-14488.
Impact Factor: 4.064
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Esposito L, Vitagliano L, Zagari A, Mazzarella L
Experimental evidence for the correlation of bond distances in peptide groups detected in ultrahigh-resolution protein structures (390 views)
Protein Eng (ISSN: 0269-2139, 0269-2139print, 0269-2139linking), 2000 Dec; 13(12): 825-828.
Impact Factor: 2.442
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D'Andrea LD, Mazzeo M, Isernia C, Rossi F, Saviano M, Gallo P, Paolillo L, Pedone C
Solution conformational preferences of a peptidic analogue of a natural macrolide (420 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1997; 42(3): 349-361.
Impact Factor: 2.425
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Pavone V, Lombardi A, Saviano M, Nastri F, Fattorusso R, Maglio O, Isernia C, Paolillo L, Pedone C
β-alanine containing cyclic peptides with turned structure: The 'pseudo type II β-turn. ' VI (684 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1994 Nov; 34(11): 1517-1526.
Impact Factor: 2.425
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Bustamante C, Gurrieri S, Pasternack RF, Purrello R, Rizzarelli E
Interaction of water-soluble porphyrins with single- and double-stranded polyribonucleotides (441 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1994 Sep; 34(8): 1099-1104.
Impact Factor: 2.425
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Romano M, Cerra M, Salvatore M, Onorati A
Effects of ionizing radiations on the activity of valyl tRNA synthetase isolated from rat liver and from Morris hepatoma 7777 (873 views)
Tumori (ISSN: 0300-8916, 0300-8916print, 0300-8916linking), 1974 Jul; 60(4): 301-306.
Impact Factor: 0.408
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33 Records (32 excluding Abstracts).
Total impact factor: 122.041 (117.949 excluding Abstracts).
Total 5 year impact factor: 162.846 (158.309 excluding Abstracts).
Total impact factor: 122.041 (117.949 excluding Abstracts).
Total 5 year impact factor: 162.846 (158.309 excluding Abstracts).
559 views. Last view on Monday 14 October 2024, 5:11:03
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