2bww
From Proteopedia
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(New page: 200px<br /> <applet load="2bww" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bww, resolution 2.61Å" /> '''HIS350ALA ESCHERICH...)
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Revision as of 15:13, 29 October 2007
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HIS350ALA ESCHERICHIA COLI AMINOPEPTIDASE P
Overview
Aminopeptidase P (APPro) is a manganese-dependent enzyme that cleaves the, N-terminal amino acid from polypeptides where the second residue is, proline. APPro shares a similar fold, substrate specificity, and catalytic, mechanism with methionine aminopeptidase and prolidase. To investigate the, roles of conserved residues at the active site, seven mutant forms of, APPro were characterized kinetically and structurally. Mutation of, individual metal ligands selectively abolished binding of either or both, Mn(II) atoms at the active site, and none of these metal-ligand mutants, had detectable catalytic activity. Mutation of the conserved active site, residues His243 and His361 revealed that both are required for catalysis., We propose that His243 stabilizes substrate binding through an ... [(full description)]
About this Structure
2BWW is a [Single protein] structure of sequence from [Escherichia coli] with MN, MG, FLC and MRD as [ligands]. Active as [[1]], with EC number [3.4.11.9]. Full crystallographic information is available from [OCA].
Reference
Kinetic and crystallographic analysis of mutant Escherichia coli aminopeptidase P: insights into substrate recognition and the mechanism of catalysis., Graham SC, Lilley PE, Lee M, Schaeffer PM, Kralicek AV, Dixon NE, Guss JM, Biochemistry. 2006 Jan 24;45(3):964-75. PMID:16411772
Page seeded by OCA on Mon Oct 29 17:17:58 2007
