Ribosomal crystallography: A flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism (635 views)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2004 Jun 1; 567(1): 20-26.
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Paper type: Journal Article,
Impact factor: 3.843, 5-year impact factor: 3.47
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-2542445275&partnerID=40&md5=029e1fe19a34de7c999989e8cc70b569
Keywords: Antibiotics Synergism, Azithromycin, Dual Binding, Peptide-Bond Formation, Positional Catalysis, Ribosome, Synercid, Amino Acid, Antibiotic Agent, Chloramphenicol, Dalfopristin Plus Quinupristin, Macrolide, Messenger Rna, Nucleotide, Streptogramin, Transfer Rna, Troleandomycin, Untranslated Region, Accuracy, Chirality, Conference Paper, Crystallography, Drug Binding, Drug Potentiation, Molecular Interaction, Nonhuman, Polymerization, Priority Journal, Protein Interaction, Protein Synthesis, Rna Transport, Rotation, Anti-Bacterial Agents, X-Ray, Models, Protein Isoforms, Protein Structure, Tertiary, Protein Transport, Substrate Specificity, Virginiamycin,
Affiliations:
*** IBB - CNR ***
Department of Structural Biology, Weizmann Institute, 76100 Rehovot, Israel
Max-Planck-Res. U. Ribosomal Struct., 22603 Hamburg, Germany
Inst. of Biostructure and Bioimaging, CNR, 80138 Naples, Italy
References:
Not available.
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2004 Jun 1; 567(1): 20-26.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.843, 5-year impact factor: 3.47
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-2542445275&partnerID=40&md5=029e1fe19a34de7c999989e8cc70b569
Keywords: Antibiotics Synergism, Azithromycin, Dual Binding, Peptide-Bond Formation, Positional Catalysis, Ribosome, Synercid, Amino Acid, Antibiotic Agent, Chloramphenicol, Dalfopristin Plus Quinupristin, Macrolide, Messenger Rna, Nucleotide, Streptogramin, Transfer Rna, Troleandomycin, Untranslated Region, Accuracy, Chirality, Conference Paper, Crystallography, Drug Binding, Drug Potentiation, Molecular Interaction, Nonhuman, Polymerization, Priority Journal, Protein Interaction, Protein Synthesis, Rna Transport, Rotation, Anti-Bacterial Agents, X-Ray, Models, Protein Isoforms, Protein Structure, Tertiary, Protein Transport, Substrate Specificity, Virginiamycin,
Affiliations:
*** IBB - CNR ***
Department of Structural Biology, Weizmann Institute, 76100 Rehovot, Israel
Max-Planck-Res. U. Ribosomal Struct., 22603 Hamburg, Germany
Inst. of Biostructure and Bioimaging, CNR, 80138 Naples, Italy
References:
Not available.
Ribosomal crystallography: A flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism
The linkage between internal ribosomal symmetry and transfer RNA (tRNA) positioning confirmed positional catalysis of amino-acid polymerization. Peptide bonds are formed concurrently with tRNA-3′end rotatory motion, in conjunction with the overall messenger RNA (mRNA)/tRNA translocation. Accurate substrate alignment, mandatory for the processivity of protein biosynthesis, is governed by remote interactions. Inherent flexibility of a conserved nucleotide, anchoring the rotatory motion, facilitates chirality discrimination and antibiotics synergism. Potential tRNA interactions explain the universality of the tRNA CCA-end and P-site preference of initial tRNA. The interactions of protein L2 tail with the symmetry-related region periphery explain its conservation and its contributions to nascent chain elongation. © 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
The linkage between internal ribosomal symmetry and transfer RNA (tRNA) positioning confirmed positional catalysis of amino-acid polymerization. Peptide bonds are formed concurrently with tRNA-3′end rotatory motion, in conjunction with the overall messenger RNA (mRNA)/tRNA translocation. Accurate substrate alignment, mandatory for the processivity of protein biosynthesis, is governed by remote interactions. Inherent flexibility of a conserved nucleotide, anchoring the rotatory motion, facilitates chirality discrimination and antibiotics synergism. Potential tRNA interactions explain the universality of the tRNA CCA-end and P-site preference of initial tRNA. The interactions of protein L2 tail with the symmetry-related region periphery explain its conservation and its contributions to nascent chain elongation. © 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
Ribosomal crystallography: A flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism
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Ribosomal crystallography: A flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism
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Zarivach R, Bashan A, Berisio R, Harms J, Auerbach T, Schluenzen F, Bartels H, Baram D, Pyetan E, Sittner A, Amit M, Hansen HAS, Kessler M, Liebe C, Wolff A, Agmon I, Yonath A
* Functional aspects of ribosomal architecture: Symmetry, chirality and regulation (849 views)
J Phys Org Chem (ISSN: 0894-3230), 2004; 17(11): 901-912.
Impact Factor: 1.211
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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 (847 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 (704 views)
Nat Struct Biol (ISSN: 1072-8368), 2003 May; 10(5): 366-370.
Impact Factor: 11.579
View Export to BibTeX Export to EndNote
* Functional aspects of ribosomal architecture: Symmetry, chirality and regulation (849 views)
J Phys Org Chem (ISSN: 0894-3230), 2004; 17(11): 901-912.
Impact Factor: 1.211
View Export to BibTeX Export to EndNote
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 (847 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2003 Sep; 70(1): 19-41.
Impact Factor: 2.733
View Export to BibTeX Export to EndNote
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 (704 views)
Nat Struct Biol (ISSN: 1072-8368), 2003 May; 10(5): 366-370.
Impact Factor: 11.579
View Export to BibTeX Export to EndNote
3 Records (3 excluding Abstracts).
Total impact factor: 15.523 (15.523 excluding Abstracts).
Total 5 year impact factor: 17.085 (17.085 excluding Abstracts).
Total impact factor: 15.523 (15.523 excluding Abstracts).
Total 5 year impact factor: 17.085 (17.085 excluding Abstracts).
635 views. Last view on Tuesday 08 April 2025, 11:27:22
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