3jtq

Mutations in Cephalosporin Acylase Affecting Stability and Autoproteolysis

spinqualitylabelsall models 3jtq, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3jtq is a 2 chain structure with sequence from Pseudomonas sp. GK16. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A4ZVL3_PSEU7 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 PubMed Cephalosporin acylase (CA), a member of the N-terminal nucleophile hydrolase family, is activated through two steps of intramolecular autoproteolysis, the first mediated by a serine residue, and the second by a glutamate, which releases the pro-segment and produces an active enzyme. In this study, we have determined the crystal structures of mutants which could affect primary or secondary auto-cleavage and of sequential intermediates of a slow-processing mutant at 2.0-2.5A resolutions. The pro-segments of the mutants undergo dynamic conformational changes during activation and adopt surprisingly different loop conformations from one another. However, the autoproteolytic site was found to form a catalytically competent conformation with a solvent water molecule, which was essentially conserved in the CA mutants. Structural features of cephalosporin acylase reveal the basis of autocatalytic activation.,Cho KJ, Kim JK, Lee JH, Shin HJ, Park SS, Kim KH Biochem Biophys Res Commun. 2009 Dec 11;390(2):342-8. Epub 2009 Oct 2. PMID:19800869 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cephalosporin acylase 3D structures

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