Crystallization and preliminary X-ray crystallographic studies of a psychrophilic subtilisin-like protease Apa1 from Antarctic Pseudoalteromonas sp. strain AS-11

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Danghong DongKeiichi Watanabe

Abstract

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.

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Citations

Jan 16, 2014·BMC Genomics·Andrea I Moreno SwittKathryn J Boor
Jan 1, 2013·Biology·Swati Joshi, Tulasi Satyanarayana
Jan 6, 2010·Critical Reviews in Microbiology·Ramesh Chand Kasana
May 11, 2019·Physics of Life Reviews·Ermenegilda ParrilliRenato Fani

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