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.
|Number of pages
|Acta Crystallographica Section F: Structural Biology and Crystallization Communications
|Published - Jan 2005
Bibliographical noteCopyright © 2005 International Union of Crystallography - http://www.iucr.org/cgi-bin/paper?za5079
- N-TERMINAL NUCLEOPHILE
- CEPHALOSPORIN ACYLASE
- HYDROLASE FAMILY