3W45

Crystal structure of RsbX in complex with cobalt in space group P1

3W45 の概要

• エントリーDOI: 10.2210/pdb3w45/pdb
• 関連するPDBエントリー: 3W40 3W41 3W42 3W43 3W44
• 分子名称: Phosphoserine phosphatase RsbX, COBALT (II) ION (3 entities in total)
• 機能のキーワード: signaling protein, gene expression regulation, stressosome, environmental stress, phosphoric monoester hydrolases, dephosphorylation, tertiary, phosphatase, hydrolase, protein phosphatase, magnesium/manganese binding, alpha-beta beta-alpha sandwich fold
• 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: 44461.92

構造登録者

Makino, M.,Teh, A.H.,Baba, S.,Shimizu, N.,Yamamoto, M.,Kumasaka, T. (登録日: 2013-01-04, 公開日: 2014-01-22, 最終更新日: 2024-03-20)

主引用文献

Teh, A.H.,Makino, M.,Hoshino, T.,Baba, S.,Shimizu, N.,Yamamoto, M.,Kumasaka, T.
Structure of the RsbX phosphatase involved in the general stress response of Bacillus subtilis
Acta Crystallogr.,Sect.D, 71:1392-1399, 2015

PubMed Abstract: In the general stress response of Bacillus subtilis, which is governed by the sigma factor σ(B), stress signalling is relayed by a cascade of Rsb proteins that regulate σ(B) activity. RsbX, a PPM II phosphatase, halts the response by dephosphorylating the stressosome composed of RsbR and RsbS. The crystal structure of RsbX reveals a reorganization of the catalytic centre, with the second Mn(2+) ion uniquely coordinated by Gly47 O from the β4-α1 loop instead of a water molecule as in PPM I phosphatases. An extra helical turn of α1 tilts the loop towards the metal-binding site, and the β2-β3 loop swings outwards to accommodate this tilting. The residues critical for this defining feature of the PPM II phosphatases are highly conserved. Formation of the catalytic centre is metal-specific, as crystallization with Mg(2+) ions resulted in a shift of the β4-α1 loop that led to loss of the second ion. RsbX also lacks the flap subdomain characteristic of PPM I phosphatases. On the basis of a stressosome model, the activity of RsbX towards RsbR-P and RsbS-P may be influenced by the different accessibilities of their phosphorylation sites.

PubMed: 26057679
DOI: 10.1107/S1399004715007166

実験手法

X-RAY DIFFRACTION (1.7 Å)