1SUL

Crystal Structure of the apo-YsxC

1SUL の概要

• エントリーDOI: 10.2210/pdb1sul/pdb
• 関連するPDBエントリー: 1SVI 1SVW
• 分子名称: GTP-binding protein YsxC (2 entities in total)
• 機能のキーワード: gtp, gtpase, gtp-binding, hydrolase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 44120.83

構造登録者

Ruzheinikov, S.N.,Das, K.S.,Sedelnikova, S.E.,Baker, P.J.,Artymiuk, P.J.,Garcia-Lara, J.,Foster, S.J.,Rice, D.W. (登録日: 2004-03-26, 公開日: 2004-05-25, 最終更新日: 2024-02-14)

主引用文献

Ruzheinikov, S.N.,Das, S.K.,Sedelnikova, S.E.,Baker, P.J.,Artymiuk, P.J.,Garcia-Lara, J.,Foster, S.J.,Rice, D.W.
Analysis of the Open and Closed Conformations of the GTP-binding Protein YsxC from Bacillus subtilis.
J.Mol.Biol., 339:265-278, 2004

PubMed Abstract: Genetic analysis has suggested that the product of the Bacillus subtilis ysxC gene is essential for survival of the microorganism and hence may represent a target for the development of a novel anti-infective agent. B.subtilis YsxC is a member of the translation factor related class of GTPases and its crystal structure has been determined in an apo form and in complex with GDP and GMPPNP/Mg2+. Analysis of these structures has allowed us to examine the conformational changes that occur during the process of nucleotide binding and GTP hydrolysis. These structural changes particularly affect parts of the switch I and switch II region of YsxC, which become ordered and disordered, respectively in the "closed" or "on" GTP-bound state and disordered and ordered, respectively, in the "open" or "off" GDP-bound conformation. Finally, the binding of the magnesium cation results in subtle shifts of residues in the G3 region, at the start of switch II, which serve to optimize the interaction with a key aspartic acid residue. The structural flexibility observed in YsxC is likely to contribute to the role of the protein, possibly allowing transduction of an essential intracellular signal, which may be mediated via interactions with a conserved patch of surface-exposed, basic residues that lies adjacent to the GTP-binding site.

PubMed: 15136032
DOI: 10.1016/j.jmb.2004.03.043

実験手法

X-RAY DIFFRACTION (2 Å)