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4A9V

Pseudomonas fluorescens PhoX

4A9V の概要
エントリーDOI10.2210/pdb4a9v/pdb
関連するPDBエントリー3ZWU
分子名称PHOX, CHLORIDE ION, LITHIUM ION, ... (8 entities in total)
機能のキーワードhydrolase, beta-propeller
由来する生物種PSEUDOMONAS FLUORESCENS
タンパク質・核酸の鎖数1
化学式量合計65502.26
構造登録者
Yong, S.C.,Roversi, P.,Lillington, J.E.D.,Zeldin, O.B.,Garman, E.F.,Lea, S.M.,Berks, B.C. (登録日: 2011-11-28, 公開日: 2012-12-05, 最終更新日: 2023-12-20)
主引用文献Yong, S.C.,Roversi, P.,Lillington, J.,Rodriguez, F.,Krehenbrink, M.,Zeldin, O.B.,Garman, E.F.,Lea, S.M.,Berks, B.C.
A Complex Iron-Calcium Cofactor Catalyzing Phosphotransfer Chemistry
Science, 345:1170-, 2014
Cited by
PubMed Abstract: Alkaline phosphatases play a crucial role in phosphate acquisition by microorganisms. To expand our understanding of catalysis by this class of enzymes, we have determined the structure of the widely occurring microbial alkaline phosphatase PhoX. The enzyme contains a complex active-site cofactor comprising two antiferromagnetically coupled ferric iron ions (Fe(3+)), three calcium ions (Ca(2+)), and an oxo group bridging three of the metal ions. Notably, the main part of the cofactor resembles synthetic oxide-centered triangular metal complexes. Structures of PhoX-ligand complexes reveal how the active-site metal ions bind substrate and implicate the cofactor oxo group in the catalytic mechanism. The presence of iron in PhoX raises the possibility that iron bioavailability limits microbial phosphate acquisition.
PubMed: 25190793
DOI: 10.1126/SCIENCE.1254237
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.1 Å)
構造検証レポート
Validation report summary of 4a9v
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-11に公開中

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