Control of ribosomal subunit rotation by elongation factor G.

Control of ribosomal subunit rotation by elongation factor G.
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DOI:
10.1126/science.1235970
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发表时间:
2013-06-28
期刊:
Science (New York, N.Y.)
影响因子:
--
通讯作者:
Cate JH
Cate JH
中科院分区:
其他
文献类型:
--
作者:
Pulk A;Cate JH

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Protein synthesis by the ribosome requires the translocation of transfer RNAs and messenger RNA by one codon after each peptide bond is formed, a reaction that requires ribosomal subunit rotation and is catalyzed by the guanosine triphosphatase (GTPase) elongation factor G (EF-G). We determined 3 Å resolution x-ray crystal structures of EF-G complexed with a non-hydrolyzable GTP analogue and bound to the Escherichia coli ribosome in different states of ribosomal subunit rotation. The structures reveal that EF-G binding to the ribosome stabilizes switch regions in the GTPase active site, resulting in a compact EF-G conformation that favors an intermediate state of ribosomal subunit rotation. These structures suggest that EF-G controls the translocation reaction by cycles of conformational rigidity and relaxation preceding and following GTP hydrolysis.
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