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4ARS

Hafnia Alvei phytase apo form

4ARS の概要
エントリーDOI10.2210/pdb4ars/pdb
関連するPDBエントリー4ARO 4ARU
分子名称HISTIDINE ACID PHOSPHATASE, GLYCEROL, ACETATE ION, ... (4 entities in total)
機能のキーワードhydrolase
由来する生物種HAFNIA ALVEI
タンパク質・核酸の鎖数1
化学式量合計46335.31
構造登録者
主引用文献Ariza, A.,Moroz, O.V.,Blagova, E.V.,Turkenburg, J.P.,Waterman, J.,Roberts, S.M.,Vind, J.,Sjoholm, C.,Lassen, S.F.,De Maria, L.,Glitsoe, V.,Skov, L.K.,Wilson, K.S.
Degradation of Phytate by the 6-Phytase from Hafnia Alvei: A Combined Structural and Solution Study.
Plos One, 8:65062-, 2013
Cited by
PubMed Abstract: Phytases hydrolyse phytate (myo-inositol hexakisphosphate), the principal form of phosphate stored in plant seeds to produce phosphate and lower phosphorylated myo-inositols. They are used extensively in the feed industry, and have been characterised biochemically and structurally with a number of structures in the PDB. They are divided into four distinct families: histidine acid phosphatases (HAP), β-propeller phytases, cysteine phosphatases and purple acid phosphatases and also split into three enzyme classes, the 3-, 5- and 6-phytases, depending on the position of the first phosphate in the inositol ring to be removed. We report identification, cloning, purification and 3D structures of 6-phytases from two bacteria, Hafnia alvei and Yersinia kristensenii, together with their pH optima, thermal stability, and degradation profiles for phytate. An important result is the structure of the H. alvei enzyme in complex with the substrate analogue myo-inositol hexakissulphate. In contrast to the only previous structure of a ligand-bound 6-phytase, where the 3-phosphate was unexpectedly in the catalytic site, in the H. alvei complex the expected scissile 6-phosphate (sulphate in the inhibitor) is placed in the catalytic site.
PubMed: 23741456
DOI: 10.1371/JOURNAL.PONE.0065062
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.9 Å)
構造検証レポート
Validation report summary of 4ars
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2024-10-30に公開中

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