2v3z | pdb_00002v3z

GLU383ALA ESCHERICHIA COLI AMINOPEPTIDASE P IN COMPLEX WITH SUBSTRATE

spinqualitylabelsall models 2v3z, resolution 1.56Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2v3z is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, MN NonStd Res: CSO Related: 1a16, 1jaw, 1m35, 1n51, 1w2m, 1w7v, 1wbq, 1wl6, 1wl9, 1wlr, 2bh3, 2bha, 2bhb, 2bhc, 2bhd, 2bn7, 2bws, 2bwt, 2bwu, 2bwv, 2bww, 2bwx, 2bwy, 2v3x, 2v3y Activity: Xaa-Pro aminopeptidase, with EC number 3.4.11.9 Resources: FirstGlance, OCA, RCSB, PDBsum 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 Aminopeptidase P (APPro) is a manganese-containing enzyme that catalyses the hydrolysis of the N-terminal residue of a polypeptide if the second residue is proline. Structures of APPro mutants with reduced or negligible activity have been determined in complex with the tripeptide substrate ValProLeu. In the complex of Glu383Ala APPro with ValProLeu one of the two metal sites is only partly occupied, indicating an essential role for Glu383 in metal binding in the presence of substrate. His361Ala APPro clearly possesses residual activity as the ValProLeu substrate has been cleaved in the crystals; difference electron density consistent with bound ProLeu dipeptide and a disordered Val amino acid is present at the active site. Contrary to previous suggestions, the His243Ala mutant is capable of binding substrate. The structure of the His243Ala APPro complex with ValProLeu shows that the peptide interacts with one of the active-site metal atoms via its terminal amino group. The implications of these complexes for the roles of the respective residues in APPro catalysis are discussed. Complexes of mutants of Escherichia coli aminopeptidase P and the tripeptide substrate ValProLeu.,Graham SC, Guss JM Arch Biochem Biophys. 2008 Jan 15;469(2):200-8. Epub 2007 Oct 24. PMID:17983589 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aminopeptidase

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