Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes

Citation
A. Wlodawer et al., Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes, NAT ST BIOL, 8(5), 2001, pp. 442-446
Citations number
35
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biochemistry & Biophysics
Journal title
NATURE STRUCTURAL BIOLOGY
ISSN journal
1072-8368 → ACNP
Volume
8
Issue
5
Year of publication
2001
Pages
442 - 446
Database
ISI
SICI code
1072-8368(200105)8:5<442:CPFPDA>2.0.ZU;2-R
Abstract
The crystal structure of a pepstatin-insensitive carboxyl proteinase from P seudomonas sp. 101 (PSCP) has been solved by single-wavelength anomalous di ffraction using the absorption peak of bromide anions. Structures of the un inhibited enzyme and of complexes with an inhibitor that was either covalen tly or noncovalently bound were refined at 1.0-1.4 Angstrom resolution. The structure of PSCP comprises a single compact domain with a diameter of sim ilar to 55 Angstrom, consisting of a seven-stranded parallel beta -sheet fl anked on both sides by a number of helices. The fold of PSCP is a superset of the subtilisin fold, and the covalently bound inhibitor is linked to the enzyme through a serine residue. Thus, the structure of PSCP defines a nov el family of serine-carboxyl proteinases (defined as MEROPS S53) with a uni que catalytic triad consisting of Glu 80, Asp 84 and Ser 287.