Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1

被引：154

作者：

Vestergaard, B

Van, LB

Andersen, GR

Nyborg, J

Buckingham, RH

Kjeldgaard, M ^{[1
]}

机构：

[1] Aarhus Univ, Inst Mol & Struct Biol, DK-8000 Aarhus C, Denmark

[2] CNRS, Inst Biol Physicochim, F-75005 Paris, France

来源：

MOLECULAR CELL | 2001年 / 8卷 / 06期

关键词：

D O I：

10.1016/S1097-2765(01)00415-4

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：

Bacterial release factor RF2 promotes termination of protein synthesis, specifically recognizing stop codons UAA or UGA. The crystal structure of Escherichia coli RF2 has been determined to a resolution of 1.8 Angstrom. RF2 is structurally distinct from its eukaryotic counterpart eRF1. The tripeptide SPF motif, thought to confer RF2 stop codon specificity, and the universally conserved GGQ motif, proposed to be involved with the peptidyl transferase center, are exposed in loops only 23 Angstrom apart, and the structure suggests that stop signal recognition is more complex than generally believed.

引用

页码：1375 / 1382

页数：8

共 22 条

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