5AA0

Complex of Thermous thermophilus ribosome (A-and P-site tRNA) bound to BipA-GDPCP

これはPDB形式変換不可エントリーです。

5AA0 の概要

• エントリーDOI: 10.2210/pdb5aa0/pdb
• EMDBエントリー: 6397
• 分子名称: 23S ribosomal RNA, 50S ribosomal protein L14, 50S ribosomal protein L15, ... (60 entities in total)
• 機能のキーワード: bipa, ribosome, translational gtpase factors, protein, x-ray crystallography and cryo-electron microscopy
• 由来する生物種: Thermus thermophilus HB8; 詳細
• タンパク質・核酸の鎖数: 58
• 化学式量合計: 2311022.80

構造登録者

Kumar, V.,Chen, Y.,Ahmed, T.,Tan, J.,Ero, R.,Bhushan, S.,Gao, Y.-G. (登録日: 2015-07-23, 公開日: 2015-10-14, 最終更新日: 2024-10-23)

主引用文献

Kumar, V.,Chen, Y.,Ero, R.,Ahmed, T.,Tan, J.,Li, Z.,Wong, A.S.W.,Bhushan, S.,Gao, Y.
Structure of Bipa in GTP Form Bound to the Ratcheted Ribosome.
Proc.Natl.Acad.Sci.USA, 112:10944-10949, 2015

PubMed Abstract: 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.

PubMed: 26283392
DOI: 10.1073/PNAS.1513216112

実験手法

ELECTRON MICROSCOPY (5 Å)