1m22: Difference between revisions

Revision as of 23:03, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1m22.png

Template:STRUCTURE 1m22

X-ray structure of native peptide amidase from Stenotrophomonas maltophilia at 1.4 AX-ray structure of native peptide amidase from Stenotrophomonas maltophilia at 1.4 A

Template:ABSTRACT PUBMED 12367528

About this StructureAbout this Structure

1M22 is a Single protein structure of sequence from Stenotrophomonas maltophilia. Full crystallographic information is available from OCA.

ReferenceReference

An alternative mechanism for amidase signature enzymes., Labahn J, Neumann S, Buldt G, Kula MR, Granzin J, J Mol Biol. 2002 Oct 4;322(5):1053-64. PMID:12367528

Page seeded by OCA on Wed Jul 2 23:03:06 2008

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OCA

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-[[Image:1m22.gif|left|200px]]
+{{Seed}}
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 {{STRUCTURE_1m22|  PDB=1m22  |  SCENE=  }}
-'''X-ray structure of native peptide amidase from Stenotrophomonas maltophilia at 1.4 A'''
+===X-ray structure of native peptide amidase from Stenotrophomonas maltophilia at 1.4 A===
-==Overview==
+<!--
-The peptide amidase from Stenotrophomonas maltophilia catalyses predominantly the hydrolysis of the C-terminal amide bond in peptide amides. Peptide bonds or amide functions in amino acid side-chains are not hydrolysed. This specificity makes peptide amidase (Pam) interesting for different biotechnological applications. Pam belongs to the amidase signature (AS) family. It is the first protein within this family whose tertiary structure has been solved. The structure of the native Pam has been determined with a resolution of 1.4A and in complex with the competitive inhibitor chymostatin at a resolution of 1.8A. Chymostatin, which forms acyl adducts with many serine proteases, binds non-covalently to this enzyme.Pam folds as a very compact single-domain protein. The AS sequence represents a core domain that is covered by alpha-helices. This AS domain contains the catalytic residues. It is topologically homologous to the phosphoinositol phosphatase domain.The structural data do not support the recently proposed Ser-Lys catalytic dyad mechanism for AS enzymes. Our results are in agreement with the role of Ser226 as the primary nucleophile but differ concerning the roles of Ser202 and Lys123: Ser202, with direct contact both to the substrate molecule and to Ser226, presumably serves as an acid/bases catalyst. Lys123, with direct contact to Ser202 but no contact to Ser226 or the substrate molecule, most likely acts as an acid catalyst.
+The line below this paragraph, {{ABSTRACT_PUBMED_12367528}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12367528 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12367528}}
 ==About this Structure==
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 [[Category: Covered double layers of alpha helices on top and bottom]]
 [[Category: Eleven-stranded beta sheet]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:32:27 2008''
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