Crystallization and preliminary X-ray crystallographic studies of a psychrophilic subtilisin-like protease Apa1 from Antarctic Pseudoalteromonas sp. strain AS-11.
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 A resolution. The crystals belong to space group C2, with unit-cell parameters a = 122.94, b = 138.48, c = 64.77 A, alpha = gamma = 90, beta = 97.5 degrees. 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.
Dong
Danghong
D
Department of Applied Biological Sciences, Saga University, Saga 840-8502, Japan.
Ihara
Tokuo
T
Motoshima
Hiroyuki
H
Watanabe
Keiichi
K
D000864:Antarctic Regions; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D031161:Pseudoalteromonas / Q000201:enzymology*; D013381:Subtilisins / Q000737:chemistry* / Q000302:isolation & purification
D001426:Bacterial Proteins; D013381:Subtilisins