3MMJ

Structure of the PTP-like phytase from Selenomonas ruminantium in complex with myo-inositol hexakisphosphate

3MMJ の概要

• エントリーDOI: 10.2210/pdb3mmj/pdb
• 関連するPDBエントリー: 2B4U
• 分子名称: Myo-inositol hexaphosphate phosphohydrolase, INOSITOL HEXAKISPHOSPHATE, PHOSPHATE ION, ... (7 entities in total)
• 機能のキーワード: phytase, protein tyrosine phosphatase, inositol phosphate, inositol phosphatase, hydrolase
• 由来する生物種: Selenomonas ruminantium
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 74585.59

構造登録者

Gruninger, R.J.,Selinger, L.B.,Mosimann, S.C. (登録日: 2010-04-20, 公開日: 2011-06-15, 最終更新日: 2023-09-06)

主引用文献

Gruninger, R.J.,Dobing, S.,Smith, A.D.,Bruder, L.M.,Selinger, L.B.,Wieden, H.J.,Mosimann, S.C.
Substrate binding in protein-tyrosine phosphatase-like inositol polyphosphatases.
J.Biol.Chem., 287:9722-9730, 2012

PubMed Abstract: Protein-tyrosine phosphatase-like inositol polyphosphatases are microbial enzymes that catalyze the stepwise removal of one or more phosphates from highly phosphorylated myo-inositols via a relatively ordered pathway. To understand the substrate specificity and kinetic mechanism of these enzymes we have determined high resolution, single crystal, x-ray crystallographic structures of inactive Selenomonas ruminantium PhyA in complex with myo-inositol hexa- and pentakisphosphate. These structures provide the first glimpse of a myo-inositol polyphosphatase-ligand complex consistent with its known specificity and reveal novel features of the kinetic mechanism. To complement the structural studies, fluorescent binding assays have been developed and demonstrate that the K(d) for this enzyme is several orders of magnitude lower than the K(m). Together with rapid kinetics data, these results suggest that the protein tyrosine phosphatase-like inositol polyphosphatases have a two-step, substrate-binding mechanism that facilitates catalysis.

PubMed: 22139834
DOI: 10.1074/jbc.M111.309872

実験手法

X-RAY DIFFRACTION (1.6 Å)