2imo

<StructureSection load='2imo' size='340' side='right' caption='[[2imo]], [[Resolution|resolution]] 2.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[2imo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IMO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IMO FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/2imo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2imo RCSB], [http://www.ebi.ac.uk/pdbsum/2imo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2imo ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/2imo TOPSAN]</span></td></tr>

== Function ==

[[http://www.uniprot.org/uniprot/ALLC_ECOLI ALLC_ECOLI]] Involved in the anaerobic utilization of allantoin. Converts allantoate to (S)-ureidoglycolate and ammonia.<ref>PMID:10601204</ref>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:17362992</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2imo" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Ecoli]]

[[Category: Agarwal, R]]

[[Category: Burley, S K]]

[[Category: Structural genomic]]

[[Category: Swaminathan, S]]

[[Category: T1507]]