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2imo

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[[Image:2imo.gif|left|200px]]
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{{Structure
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|GENE= allC_ecoli ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK12893 PRK12893], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK09290 PRK09290]</span>
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{{STRUCTURE_2imo| PDB=2imo | SCENE= }}
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|RELATEDENTRY=[[1z2l|1Z2L]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2imo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2imo OCA], [http://www.ebi.ac.uk/pdbsum/2imo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2imo RCSB]</span>
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'''Crystal structure of allantoate amidohydrolase from Escherichia coli at pH 4.6'''
'''Crystal structure of allantoate amidohydrolase from Escherichia coli at pH 4.6'''
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[[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]]
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[[Category: Swaminathan, S.]]
[[Category: Swaminathan, S.]]
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[[Category: allantoate amidohydrolase]]
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[[Category: Allantoate amidohydrolase]]
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[[Category: allc]]
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[[Category: apoenzyme]]
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[[Category: new york structural genomix research consortium]]
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[[Category: structural genomic]]
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[[Category: Structural genomic]]
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Revision as of 04:39, 4 May 2008

Image:2imo.gif

Template:STRUCTURE 2imo

Crystal structure of allantoate amidohydrolase from Escherichia coli at pH 4.6


Overview

Purine metabolism plays a major role in regulating the availability of purine nucleotides destined for nucleic acid synthesis. Allantoate amidohydrolase catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. The crystal structure of a ternary complex of allantoate amidohydrolase with its substrate allantoate and an allosteric effector, a sulfate ion, from Escherichia coli was determined to understand better the catalytic mechanism and substrate specificity. The 2.25 A resolution X-ray structure reveals an alpha/beta scaffold akin to zinc exopeptidases of the peptidase M20 family and lacks the (beta/alpha)(8)-barrel fold characteristic of the amidohydrolases. Arrangement of the substrate and the two co-catalytic zinc ions at the active site governs catalytic specificity for hydrolysis of N-carbamyl versus the peptide bond in exopeptidases. In its crystalline form, allantoate amidohydrolase adopts a relatively open conformation. However, structural analysis reveals the possibility of a significant movement of domains via rotation about two hinge regions upon allosteric effector and substrate binding resulting in a closed catalytically competent conformation by bringing the substrate allantoate closer to co-catalytic zinc ions. Two cis-prolyl peptide bonds found on either side of the dimerization domain in close proximity to the substrate and ligand-binding sites may be involved in protein folding and in preserving the integrity of the catalytic site.

About this Structure

2IMO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural analysis of a ternary complex of allantoate amidohydrolase from Escherichia coli reveals its mechanics., Agarwal R, Burley SK, Swaminathan S, J Mol Biol. 2007 Apr 27;368(2):450-63. Epub 2007 Feb 20. PMID:17362992 Page seeded by OCA on Sun May 4 07:39:52 2008

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