2HJG

The crystal structure of the B. subtilis YphC GTPase in complex with GDP

2HJG の概要

• エントリーDOI: 10.2210/pdb2hjg/pdb
• 関連するPDBエントリー: 1MKY
• 分子名称: GTP-binding protein engA, ZINC ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: gtpase enga kh-domain, hydrolase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 50343.05

構造登録者

Muench, S.P.,Xu, L.,Sedelnikova, S.E.,Rice, D.W. (登録日: 2006-06-30, 公開日: 2006-08-08, 最終更新日: 2024-11-20)

主引用文献

Muench, S.P.,Xu, L.,Sedelnikova, S.E.,Rice, D.W.
The essential GTPase YphC displays a major domain rearrangement associated with nucleotide binding.
Proc.Natl.Acad.Sci.Usa, 103:12359-12364, 2006

PubMed Abstract: The structure of a Bacillus subtilis YphC/GDP complex shows that it contains two GTPase domains that pack against a central domain whose fold resembles that of an RNA binding KH-domain. Comparisons of this structure to that of a homologue in Thermotoga maritima reveals a dramatic rearrangement in the position of the N-terminal GTPase domain with a shift of up to 60 A and the formation of a totally different interface to the central domain. This rearrangement appears to be triggered by conformational changes of the switch II region in this domain in response to nucleotide binding. Modeling studies suggest that this motion represents transitions between the "on" and "off" states of the GTPase, the effect of which is to alternately expose and bury a positively charged face of the central domain that we suggest is involved in RNA recognition as part of the possible role of this enzyme in ribosome binding.

PubMed: 16894162
DOI: 10.1073/pnas.0602585103

実験手法

X-RAY DIFFRACTION (2.5 Å)