Open AccessCrystallization and preliminary X‐ray crystallographic studies of Pz peptidase A from Geobacillus collagenovorans MO‐1
Author(s) -
Nakano Hiroaki,
Kato Hiroaki,
Kawasaki Akio,
Matsui Hiroshi,
Tsujimoto Yoshiyuki,
Shimizu Tetsuya,
Nakatsu Toru,
Watanabe Kunihiko
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910700334x
Subject(s) - tripeptide , enzyme , chemistry , stereochemistry , thermophile , crystallization , crystallography , biochemistry , peptide , organic chemistry
Pz peptidase A is an intracellular M3 metallopeptidase found in the thermophile Geobacillus collagenovorans MO‐1 that recognizes collagen‐specific tripeptide units (Gly‐Pro‐Xaa). Pz peptidase A shares common reactions with mammalian thimet oligopeptidase (TOP) and neurolysin, but has extremely low primary sequence identity to these enzymes. In this work, Pz peptidase A was cocrystallized with a phosphine peptide inhibitor (PPI) that selectively inhibits TOP and neurolysin. The crystals belong to space group P 2 1 , with unit‐cell parameters a = 56.38, b = 194.15, c = 59.93 Å, β = 106.22°. This is the first crystallographic study of an M3 family peptidase–PPI complex.