Document Detail

Changes in the level of poly(Phe) synthesis in Escherichia coli ribosomes containing mutants of L4 ribosomal protein from Thermus thermophilus can be explained by structural changes in the peptidyltransferase center: a molecular dynamics simulation analysis.
MedLine Citation:
PMID:  16773394     Owner:  NLM     Status:  MEDLINE    
Data from polyphenylalanine [poly(Phe)] synthesis determination in the presence and in the absence of erythromycin have been used in conjunction with Molecular Dynamics Simulation analysis, in order to localize the functional sites affected by mutations of Thermus thermophilus ribosomal protein L4 incorporated in Escherichia coli ribosomes. We observed that alterations in ribosome capability to synthesize poly(Phe) in the absence of erythromycin were mainly correlated to shifts of A2062 and C2612 of 23S rRNA, while in the presence of erythromycin they were correlated to shifts of A2060 and U2584 of 23S rRNA. Our results suggest a means of understanding the role of the extended loop of L4 ribosomal protein in ribosomal peptidyltransferase center.
G Papadopoulos; S Grudinin; D L Kalpaxis; T Choli-Papadopoulou
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Publication Detail:
Type:  Journal Article     Date:  2006-06-14
Journal Detail:
Title:  European biophysics journal : EBJ     Volume:  35     ISSN:  0175-7571     ISO Abbreviation:  Eur. Biophys. J.     Publication Date:  2006 Oct 
Date Detail:
Created Date:  2006-09-29     Completed Date:  2007-04-27     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8409413     Medline TA:  Eur Biophys J     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  675-83     Citation Subset:  IM    
Department of Biochemistry and Biotechnology, University of Thessaly, Ploutonos 26, 41221, Larissa, Greece.
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MeSH Terms
Amino Acid Sequence
Anti-Bacterial Agents / pharmacology
Erythromycin / pharmacology
Escherichia coli / drug effects,  genetics,  metabolism*
Models, Molecular
Molecular Sequence Data
Nucleic Acid Conformation
Peptides / metabolism*
Peptidyl Transferases / chemistry,  metabolism*
Protein Conformation
RNA, Bacterial / genetics
RNA, Ribosomal, 23S / genetics
Ribosomal Proteins / chemistry,  genetics*,  metabolism
Ribosomes / genetics,  metabolism*
Thermus thermophilus / metabolism*
Reg. No./Substance:
0/Anti-Bacterial Agents; 0/Peptides; 0/RNA, Bacterial; 0/RNA, Ribosomal, 23S; 0/Ribosomal Proteins; 0/ribosomal protein L4; 114-07-8/Erythromycin; 30394-07-1/polyphenylalanine; EC Transferases

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