Open AccessCrystallization and preliminary X‐ray crystallographic studies of a psychrophilic subtilisin‐like protease Apa1 from Antarctic Pseudoalteromonas sp. strain AS‐11
Author(s) -
Dong Danghong,
Ihara Tokuo,
Motoshima Hiroyuki,
Watanabe Keiichi
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105004082
Subject(s) - psychrophile , subtilisin , serine protease , crystallography , protease , crystallization , chemistry , mesophile , protein data bank (rcsb pdb) , biochemistry , stereochemistry , biology , enzyme , bacteria , organic chemistry , genetics
The psychrophilic alkaline serine protease Apa1 secreted by the Antarctic psychrotroph Pseudoalteromonas sp. strain AS‐11 consists of a subtilisin‐like region (293 residues) and an additional insert region (148 residues) that does not show a sequence homology to any proteins in the RCSB Protein Data Bank. Apa1 inhibited with phenylmethanesulfonyl fluoride has been crystallized and X‐ray diffraction data have been collected to 1.78 Å resolution. The crystals belong to space group C 2, with unit‐cell parameters a = 122.94, b = 138.48, c = 64.77 Å, α = γ = 90, β = 97.5°. A molecular‐replacement solution has been found using the structure of the mesophilic counterpart subtilisin DY with 38% sequence identity to the catalytic domain of Apa1 as a search model. This is the first crystallographic study of a cold‐adapted subtilisin‐like protease.