Open AccessCrystallization and preliminary X‐ray crystallographic analysis of Pz peptidase B from Geobacillus collagenovorans MO‐1
Author(s) -
Nakano Hiroaki,
Hosokawa Allin,
Tagawa Ryuji,
Inaka Koji,
Ohta Kazunori,
Nakatsu Toru,
Kato Hiroaki,
Watanabe Kunihiko
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112018969
Subject(s) - crystallography , tripeptide , crystallization , chemistry , stereochemistry , cleavage (geology) , peptide , biochemistry , materials science , organic chemistry , fracture (geology) , composite material
Pz peptidase B is an intracellular M3 metallopeptidase that is found together with Pz peptidase A in the thermophile Geobacillus collagenovorans MO‐1 and recognizes collagen‐specific tripeptide units (‐Gly‐Pro‐ X ‐). These peptidases have low homology in their primary structures; however, their cleavage patterns towards peptide substrates are similar. In this work, Pz peptidase B was crystallized using the counter‐diffusion method. Data were collected to a resolution of 1.6 Å at 100 K from a crystal obtained in the Japanese Experiment Module (JEM; also known as `Kibo') at the International Space Station (ISS). The crystal belonged to the trigonal space group P 3 1 21, with unit‐cell parameters a = b = 87.64, c = 210.5 Å. A complete data set was also obtained from crystals of selenomethionine‐substituted protein.