The 2′-OH group of the peptidyl-tRNA stabilizes an active conformation of the ribosomal PTC

EMBO Journal

Volumn 30, Issue 12, 2011, Pages 2445-2453

  Zaher, Hani S ^a   Shaw, Jeffrey J ^a   Strobel, Scott A ^b   Green, Rachel ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b YALE UNIVERSITY   (United States)

Author keywords

2 OH; mechanism; peptidyl transfer; peptidyl tRNA; ribosome

Indexed keywords

ELONGATION FACTOR TU; HYDROXYL GROUP; PEPTIDE; PEPTIDE TRANSFER RIBONUCLEIC ACID; PEPTIDYLTRANSFERASE; TRANSFER RNA; UNCLASSIFIED DRUG; AMINOACYL TRANSFER RNA; HYDROXYL RADICAL; OXIDIZING AGENT;

ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; NONHUMAN; PRIORITY JOURNAL; REACTION ANALYSIS; REACTION TIME; RIBOSOME; CHEMICAL MODEL; CHEMISTRY; CONFORMATION; ENZYME SPECIFICITY; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; HYDROGEN BOND; METABOLISM; NUCLEOTIDE SEQUENCE; PROTEIN STABILITY; RNA TRANSLATION;

CATALYSIS; CATALYTIC DOMAIN; CONSERVED SEQUENCE; ESCHERICHIA COLI; HYDROGEN BONDING; HYDROXYL RADICAL; MODELS, CHEMICAL; NUCLEIC ACID CONFORMATION; OXIDANTS; PEPTIDE CHAIN ELONGATION, TRANSLATIONAL; PROTEIN STABILITY; RIBOSOMES; RNA, TRANSFER, AMINO ACYL; SUBSTRATE SPECIFICITY;

EID: 79958829880     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2011.142     Document Type: Article

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