View source for 2imo

[[Image:2imo.gif|left|200px]]

 {{Structure
|PDB= 2imo |SIZE=350|CAPTION= <scene name='initialview01'>2imo</scene>, resolution 2.80&Aring;
|SITE= 
|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
|ACTIVITY= 
|GENE= allC_ecoli ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|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>
|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>
}}

'''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 [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IMO 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:[http://www.ncbi.nlm.nih.gov/pubmed/17362992 17362992]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Agarwal, R.]]
[[Category: Burley, S K.]]
[[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]]
[[Category: Swaminathan, S.]]
[[Category: allantoate amidohydrolase]]
[[Category: allc]]
[[Category: apoenzyme]]
[[Category: new york structural genomix research consortium]]
[[Category: nysgxrc]]
[[Category: protein structure initiative]]
[[Category: psi-2]]
[[Category: structural genomic]]
[[Category: t1507]]

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