2bww
From Proteopedia
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| - | [[Image:2bww.gif|left|200px]]<br /><applet load="2bww" size=" | + | [[Image:2bww.gif|left|200px]]<br /><applet load="2bww" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2bww, resolution 2.61Å" /> | caption="2bww, resolution 2.61Å" /> | ||
'''HIS350ALA ESCHERICHIA COLI AMINOPEPTIDASE P'''<br /> | '''HIS350ALA ESCHERICHIA COLI AMINOPEPTIDASE P'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BWW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MN, MG, FLC and MRD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Xaa-Pro_aminopeptidase Xaa-Pro aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.9 3.4.11.9] Known structural/functional Site: <scene name='pdbsite=AC1:Mrd Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | + | 2BWW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=FLC:'>FLC</scene> and <scene name='pdbligand=MRD:'>MRD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Xaa-Pro_aminopeptidase Xaa-Pro aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.9 3.4.11.9] Known structural/functional Site: <scene name='pdbsite=AC1:Mrd+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BWW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: proline-specific enzyme]] | [[Category: proline-specific enzyme]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:28:45 2008'' |
Revision as of 08:28, 3 February 2008
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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 interaction, with the carbonyl oxygen of the requisite proline residue of a substrate, and that His361 stabilizes substrate binding and the gem-diol catalytic, intermediate. Sequence, structural, and kinetic analyses reveal that, His350, conserved in APPro and prolidase but not in methionine, aminopeptidase, forms part of a hydrophobic binding pocket that gives, APPro its proline specificity. Further, peptides in which the required, proline residue is replaced by N-methylalanine or alanine are cleaved by, APPro, but they are extremely poor substrates due to a loss of, interactions between the prolidyl ring of the substrate and the, hydrophobic proline-binding pocket.
About this Structure
2BWW is a Single protein structure of sequence from Escherichia coli with , , and as ligands. Active as Xaa-Pro aminopeptidase, with EC number 3.4.11.9 Known structural/functional Site: . 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
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