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PRECURSOR MUTANT CYS1SER OF PENICILLIN V ACYLASE FROM BACILLUS SPHAERICUSPRECURSOR MUTANT CYS1SER OF PENICILLIN V ACYLASE FROM BACILLUS SPHAERICUS
Structural highlights
Function[PAC_LYSSH] The enzyme catalyzes the conversion of penicillin to 6-aminopenicillanate The precursor, furthermore, acts as a self-processing peptidase that cleaves off the propeptide. All peptidase activity is lost on conversion to the mature peptidase. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystallization of three catalytically inactive mutants of penicillin V acylase (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 three-dimensional structures of precursor PVA forms, plus open a route to the study of enzyme-substrate complexes for this industrially important enzyme. Cloning, preparation and preliminary crystallographic studies of penicillin V acylase autoproteolytic processing mutants.,Chandra PM, Brannigan JA, Prabhune A, Pundle A, Turkenburg JP, Dodson GG, Suresh CG Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jan 1;61(Pt, 1):124-7. Epub 2004 Dec 24. PMID:16508111[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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