2v3y

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{{STRUCTURE_2v3y| PDB=2v3y | SCENE= }}
{{STRUCTURE_2v3y| PDB=2v3y | SCENE= }}
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'''HIS361ALA ESCHERICHIA COLI AMINOPEPTIDASE P IN COMPLEX WITH PRODUCT'''
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===HIS361ALA ESCHERICHIA COLI AMINOPEPTIDASE P IN COMPLEX WITH PRODUCT===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 17983589 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17983589}}
==About this Structure==
==About this Structure==
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[[Category: Proline- specific enzyme]]
[[Category: Proline- specific enzyme]]
[[Category: Protease]]
[[Category: Protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:10:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:06:23 2008''

Revision as of 06:06, 28 July 2008

Image:2v3y.png

Template:STRUCTURE 2v3y

HIS361ALA ESCHERICHIA COLI AMINOPEPTIDASE P IN COMPLEX WITH PRODUCT

Template:ABSTRACT PUBMED 17983589

About this Structure

2V3Y is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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

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