3mji | pdb_00003mji

Activation of catalytic cysteine without a base in a Mutant Penicillin Acylase Precursor

spinqualitylabelsall models 3mji, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3mji is a 4 chain structure with sequence from Atcc 14577. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2pva, 3pva, 2quy, 2z71, 3mik Activity: Penicillin amidase, with EC number 3.5.1.11 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. Publication Abstract from PubMed The 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Penicillin acylase

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