Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome.
Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome.
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DOI：
10.1038/nsmb.1577
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发表时间：
2009-05
影响因子：
16.8
通讯作者：
中科院分区：
文献类型：
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蛋白质的合成是在位于核糖体大（50S）亚基的肽基转移酶中心（PTC）催化的。完整核糖体的高分辨率结构没有包含包括a -和p -位点trna的完整活性位点。此外，尽管50S亚基的结构在PTC上没有发现有序蛋白，但生化证据表明特定蛋白能够与tRNA配体的3 '端相互作用。在这里，我们展示了分辨率为3.5 Å和3.55 Å的70S核糖体与A-位点和p -位点trna复合物的结构，模拟肽基前和后转移状态。这些结构表明，PTC在50S亚基和完整的核糖体之间非常相似。此外，它们揭示了核糖体蛋白L16和L27与tRNA底物之间的相互作用，有助于阐明这些蛋白在肽基转移中的作用。
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. Additionally, though structures of the 50S subunit found no ordered proteins at the PTC, biochemical evidence suggests specific proteins are capable of interacting with the 3′ ends of the tRNA ligands. Here we present structures at 3.5 Å and 3.55 Å resolution 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. Additionally they reveal interactions between ribosomal proteins L16 and L27 and the tRNA substrates, helping to elucidate the role of these proteins in peptidyl transfer.
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DOI：
10.1073/pnas.071527498
发表时间：
2001-03-27
影响因子：
11.1
作者：
Belova, L;Tenson, T;Mankin, AS
通讯作者：
Mankin, AS
影响因子：
64.8
作者：
Laurberg, Martin;Asahara, Haruichi;Noller, Harry F.
通讯作者：
Noller, Harry F.
影响因子：
2.9
作者：
LILL, R;ROBERTSON, JM;WINTERMEYER, W
通讯作者：
WINTERMEYER, W
影响因子：
3.6
作者：
Robins, MJ;Miles, RW;Kaspar, RL
通讯作者：
Kaspar, RL
DOI：
10.1107/s0907444998003254
发表时间：
1998-09-01
期刊：
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
影响因子：
--
作者：
Brunger, AT;Adams, PD;Warren, GL
通讯作者：
Warren, GL