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Crystallization and Preliminary X-ray Crystallographic Studies of a Psychrophilic Subtilisin-Like Protease Apa1 From Antarctic Pseudoalteromonas Sp. Strain AS-11

Crystallization and Preliminary X-ray Crystallographic Studies of a Psychrophilic Subtilisin-Like Protease Apa1 From Antarctic Pseudoalteromonas Sp. Strain AS-11

Danghong Dong, Tokuo Ihara, Hiroyuki Motoshima, Keiichi Watanabe

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Mar 1;61(Pt 3):308-11.

PMID: 16511027

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP329986-A	Phenylmethanesulfonyl fluoride solution		329-98-6	Price

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