3A9L

Structure of Bacteriophage poly-gamma-glutamate hydrolase

3A9L の概要

• エントリーDOI: 10.2210/pdb3a9l/pdb
• 分子名称: Poly-gamma-glutamate hydrolase, ZINC ION, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: zinc ion binding, open alpha/beta mixed core structure, hydrolase
• 由来する生物種: Bacillus phage phiNIT1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48388.06

構造登録者

Fujimoto, Z.,Kimura, K. (登録日: 2009-10-30, 公開日: 2010-11-10, 最終更新日: 2024-03-13)

主引用文献

Fujimoto, Z.,Kimura, K.
Crystal structure of bacteriophage PhiNIT1 zinc peptidase PghP that hydrolyzes gamma-glutamyl linkage of bacterial poly-gamma-glutamate
Proteins, 80:722-732, 2012

PubMed Abstract: Poly-γ-glutamate hydrolase P (PghP) of Bacillus subtilis bacteriophage ΦNIT1 hydrolyzes the γ-glutamyl peptide linkage of extracellular poly-γ-glutamate produced by bacilli, which facilitates infection and propagation of phage progenies. Crystal structure of PghP was determined at a resolution of 1.9 Å. Structure of PghP was elucidated as a globular protein with an open α/β mixed core structure and a seven-stranded parallel/anti-parallel β-sheet. The β-sheet contained a core four-stranded parallel β-sheet. A zinc-binding motif, His-Glu-His, was identified at the C-terminal end of the β-sheet. Structure analysis demonstrated that PghP, which had not been previously classified into any peptidase/protease family due to lack of amino acid sequence similarity with known enzymes, had a catalytic center containing a zinc ion and an overall topology resembling mammalian carboxypeptidase A and related enzymes. Structural comparisons indicated important amino acid residues of PghP for catalysis and recognition of the γ-peptide bond of poly-γ-glutamate, which was confirmed by site-directed mutagenesis of PghP.

PubMed: 22105902
DOI: 10.1002/prot.23229

実験手法

X-RAY DIFFRACTION (1.9 Å)