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| [[Image:2v3z.jpg|left|200px]] | | {{Seed}} |
| | [[Image:2v3z.png|left|200px]] |
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| {{STRUCTURE_2v3z| PDB=2v3z | SCENE= }} | | {{STRUCTURE_2v3z| PDB=2v3z | SCENE= }} |
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| '''GLU383ALA ESCHERICHIA COLI AMINOPEPTIDASE P IN COMPLEX WITH SUBSTRATE'''
| | ===GLU383ALA ESCHERICHIA COLI AMINOPEPTIDASE P IN COMPLEX WITH SUBSTRATE=== |
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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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17983589}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17983589 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17983589}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Proline- specific enzyme]] | | [[Category: Proline- specific enzyme]] |
| [[Category: Protease]] | | [[Category: Protease]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:10:52 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:37:45 2008'' |
