Structure of BipA in GTP form bound to the ratcheted ribosome

被引：31

作者：

Kumar, Veerendra ^{[1
,2
]}

Chen, Yun ^{[2
]}

Ero, Rya ^{[2
]}

Ahmed, Tofayel ^{[2
]}

Tan, Jackie ^{[2
]}

Li, Zhe ^{[1
]}

Wong, Andrew See Weng ^{[2
]}

Bhushan, Shashi ^{[2
]}

Gao, Yong-Gui ^{[1
,2
]}

机构：

[1] ASTAR, Inst Mol & Cell Biol, Singapore 138673, Singapore

[2] Nanyang Technol Univ, Sch Biol Sci, Singapore 637551, Singapore

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2015年 / 112卷 / 35期

基金：

新加坡国家研究基金会;

关键词：

BipA; ribosome; translational GTPase factors; X-ray crystallography; cryo-electron microscopy; ELONGATION-FACTOR-G; TRANSFER-RNA TRANSLOCATION; ESCHERICHIA-COLI; CRYSTAL-STRUCTURE; EF-G; PRETRANSLOCATION STATE; ELECTRON-MICROSCOPY; PROTEIN-SYNTHESIS; CRYO-EM; BINDING;

D O I：

10.1073/pnas.1513216112

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

BPI-inducible protein A (BipA) is a member of the family of ribosome-dependent translational GTPase (trGTPase) factors along with elongation factors G and 4 (EF-G and EF4). Despite being highly conserved in bacteria and playing a critical role in coordinating cellular responses to environmental changes, its structures (isolated and ribosome bound) remain elusive. Here, we present the crystal structures of apo form and GTP analog, GDP, and guanosine-3',5'-bisdiphosphate (ppGpp)-bound BipA. In addition to having a distinctive domain arrangement, the C-terminal domain of BipA has a unique fold. Furthermore, we report the cryo-electron microscopy structure of BipA bound to the ribosome in its active GTP form and elucidate the unique structural attributes of BipA interactions with the ribosome and A-site tRNA in the light of its possible function in regulating translation.

引用

页码：10944 / 10949

页数：6

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