Cloning, preparation and preliminary crystallographic studies of penicillin V acylase autoproteolytic processing mutants

Chandra, P M, Brannigan, J A, Prabhune, A, Pundle, A, Turkenburg, J P, Dodson, G G and Suresh, C G (2005) Cloning, preparation and preliminary crystallographic studies of penicillin V acylase autoproteolytic processing mutants. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. pp. 124-127. ISSN 1744-3091

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Published Version: http://dx.doi.org/10.1107/S1744309104031227

Abstract

The crystallization of three catalytically inactive mutants of penicillin Vacylase (PVA) from Bacillus sphaericus in precursor and processed forms is reported. The mutant proteins crystallize in different primitive monoclinic space groups that are distinct from the crystal forms for the native enzyme. Directed mutants and clone constructs were designed to study the post-translational autoproteolytic processing of PVA. The catalytically inactive mutants will provide threedimensional structures of precursor PVA forms, plus open a route to the study of enzyme-substrate complexes for this industrially important enzyme.

Item Type:	Article
Copyright, Publisher and Additional Information:	Copyright © 2005 International Union of Crystallography - http://www.iucr.org/cgi-bin/paper?za5079
Keywords:	N-TERMINAL NUCLEOPHILE, CEPHALOSPORIN ACYLASE, BACILLUS-SPHAERICUS, CRYSTAL-STRUCTURES, HYDROLASE FAMILY, ACTIVATION, ACID, INSIGHTS, REVEALS, ENZYME
Academic Units:	The University of York > Chemistry (York)
Depositing User:	Sherpa Assistant
Date Deposited:	11 May 2005
Last Modified:	19 Feb 2013 11:50
Published Version:	http://dx.doi.org/10.1107/S1744309104031227
Status:	Published
Refereed:	Yes
Related URLs:	http://www.iucr.org/cgi-bin/paper?za5079
URI:	http://eprints.whiterose.ac.uk/id/eprint/460

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