Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome

被引:281
作者
Voorhees, Rebecca M. [1 ]
Weixlbaumer, Albert [1 ]
Loakes, David [1 ]
Kelley, Ann C. [1 ]
Ramakrishnan, V. [1 ]
机构
[1] MRC, Mol Biol Lab, Cambridge CB2 2QH, England
基金
英国医学研究理事会; 英国惠康基金;
关键词
AMINOACYLATED TRANSFER-RNAS; ESCHERICHIA-COLI; BOND FORMATION; PROTEIN L27; P-SITE; STRUCTURAL BASIS; ANGSTROM RESOLUTION; MASS-SPECTROMETRY; A-SITE; SUBUNIT;
D O I
10.1038/nsmb.1577
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Protein synthesis is catalyzed in the peptidyl transferase center (PTC), located in the large (50S) subunit of the ribosome. No high-resolution structure of the intact ribosome has contained a complete active site including both A- and P-site tRNAs. In addition, although past structures of the 50S subunit have found no ordered proteins at the PTC, biochemical evidence suggests that specific proteins are capable of interacting with the 3' ends of tRNA ligands. Here we present structures, at 3.6-angstrom and 3.5-angstrom resolution respectively, of the 70S ribosome in complex with A- and P-site tRNAs that mimic pre- and post-peptidyl-transfer states. These structures demonstrate that the PTC is very similar between the 50S subunit and the intact ribosome. They also reveal interactions between the ribosomal proteins L16 and L27 and the tRNA substrates, helping to elucidate the role of these proteins in peptidyl transfer.
引用
收藏
页码:528 / 533
页数:6
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