1H2F

BACILLUS STEAROTHERMOPHILUS PHOE (previously known as yhfr) in complex with trivanadate

1H2F の概要

• エントリーDOI: 10.2210/pdb1h2f/pdb
• 関連するPDBエントリー: 1EBB 1H2E
• 分子名称: PHOSPHATASE, TRIVANADATE, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: hydrolase, broad specificity phosphatase; dpgm homolog
• 由来する生物種: BACILLUS STEAROTHERMOPHILUS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24023.47

構造登録者

Rigden, D.J.,Littlejohn, J.E.,Jedrzejas, M.J. (登録日: 2002-08-08, 公開日: 2002-08-12, 最終更新日: 2024-11-06)

主引用文献

Rigden, D.J.,Littlejohn, J.E.,Henderson, K.,Jedrzejas, M.J.
Structures of Phosphate and Trivanadate Complexes of Bacillus Stearothermophilus Phosphatase Phoe: Structural and Functional Analysis in the Cofactor-Dependent Phosphoglycerate Mutase Superfamily
J.Mol.Biol., 325:411-, 2003

PubMed Abstract: Bacillus stearothermophilus phosphatase PhoE is a member of the cofactor-dependent phosphoglycerate mutase superfamily possessing broad specificity phosphatase activity. Its previous structural determination in complex with glycerol revealed probable bases for its efficient hydrolysis of both large, hydrophobic, and smaller, hydrophilic substrates. Here we report two further structures of PhoE complexes, to higher resolution of diffraction, which yield a better and thorough understanding of its catalytic mechanism. The environment of the phosphate ion in the catalytic site of the first complex strongly suggests an acid-base catalytic function for Glu83. It also reveals how the C-terminal tail ordering is linked to enzyme activation on phosphate binding by a different mechanism to that seen in Escherichia coli phosphoglycerate mutase. The second complex structure with an unusual doubly covalently bound trivanadate shows how covalent modification of the phosphorylable His10 is accompanied by small structural changes, presumably to catalytic advantage. When compared with structures of related proteins in the cofactor-dependent phosphoglycerate mutase superfamily, an additional phosphate ligand, Gln22, is observed in PhoE. Functional constraints lead to the corresponding residue being conserved as Gly in fructose-2,6-bisphosphatases and Thr/Ser/Cys in phosphoglycerate mutases. A number of sequence annotation errors in databases are highlighted by this analysis. B. stearothermophilus PhoE is evolutionarily related to a group of enzymes primarily present in Gram-positive bacilli. Even within this group substrate specificity is clearly variable highlighting the difficulties of computational functional annotation in the cofactor-dependent phosphoglycerate mutase superfamily.

PubMed: 12498792
DOI: 10.1016/S0022-2836(02)01229-9

実験手法

X-RAY DIFFRACTION (2 Å)