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1.2 Å crystal structure of the serine carboxyl proteinase pro-kumamolisin

Comellas-Bigler, Mireia, Maskos, Klaus, Huber, Robert, Oyama, Hiroshi, Oda, Kohei and Bode, Wolfram 2004. 1.2 Å crystal structure of the serine carboxyl proteinase pro-kumamolisin. Structure 12 (7) , pp. 1313-1323. 10.1016/j.str.2004.04.013

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Abstract

Kumamolisin, an extracellular proteinase derived from an acido/thermophilic Bacillus, belongs to the sedolisin family of endopeptidases characterized by a subtilisin-like fold and a Ser-Glu-Asp catalytic triad. In kumamolisin, the Asp82 carboxylate hydrogen bonds to Glu32-Trp129, which might act as a proton sink stabilizing the catalytic residues. The 1.2/1.3 Å crystal structures of the Glu32→Ala and Trp129→Ala mutants show that both mutations affect the active-site conformation, causing a 95% activity decrease. In addition, the 1.2 Å crystal structure of the Ser278→Ala mutant of pro-kumamolisin was determined. The prodomain exhibits a half-β sandwich core docking to the catalytic domain similarly as the equivalent subtilisin prodomains in their catalytic-domain complexes. This pro-kumamolisin structure displays, for the first time, the uncleaved linker segment running across the active site and connecting the prodomain with the properly folded catalytic domain. The structure strongly points to an initial intramolecular activation cleavage in subtilases, as presumed for pro-subtilisin and pro-furin.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Publisher: Elsevier
ISSN: 0969-2126
Last Modified: 24 Jun 2017 11:00
URI: http://orca-mwe.cf.ac.uk/id/eprint/70161

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