2V3Z

Glu383Ala Escherichia coli aminopeptidase P in complex with substrate

Summary for 2V3Z

• Entry DOI: 10.2210/pdb2v3z/pdb
• 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
• Descriptor: XAA-PRO AMINOPEPTIDASE, TRIPEPTIDE (VALINE-PROLINE-LEUCINE), MANGANESE (II) ION, ... (5 entities in total)
• Functional Keywords: 'pita-bread' enzyme, proline- specific enzyme, aminopeptidase p, manganese enzyme, protease, manganese, hydrolase, metal-binding, metalloenzyme, aminopeptidase, metalloprotease
• Biological source: ESCHERICHIA COLI; More
• Total number of polymer chains: 2
• Total formula weight: 50174.78

Authors

Graham, S.C.,Guss, J.M. (deposition date: 2007-06-25, release date: 2007-11-20, Last modification date: 2024-10-23)

Primary citation

Graham, S.C.,Guss, J.M.
Complexes of Mutants of Escherichia Coli Aminopeptidase P and the Tripeptide Substrate Valproleu.
Arch.Biochem.Biophys., 469:200-, 2008

PubMed Abstract: 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.

PubMed: 17983589
DOI: 10.1016/J.ABB.2007.10.009

Experimental method

X-RAY DIFFRACTION (1.56 Å)