2imo

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|PDB= 2imo |SIZE=350|CAPTION= <scene name='initialview01'>2imo</scene>, resolution 2.80&Aring;
|PDB= 2imo |SIZE=350|CAPTION= <scene name='initialview01'>2imo</scene>, resolution 2.80&Aring;
|SITE=
|SITE=
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|LIGAND=
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= allC_ecoli ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|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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|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.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=2imo RCSB]</span>
}}
}}
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[[Category: t1507]]
[[Category: t1507]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:31:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 06:32:32 2008''

Revision as of 04:32, 26 March 2008

Image:2imo.gif


PDB ID 2imo

Drag the structure with the mouse to rotate
, resolution 2.80Å
Ligands:
Gene: allC_ecoli (Escherichia coli)
Domains: PRK12893, PRK09290
Resources: FirstGlance, OCA, PDBsum, JenaLib, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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