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2imo

From Proteopedia

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(New page: 200px<br /><applet load="2imo" size="450" color="white" frame="true" align="right" spinBox="true" caption="2imo, resolution 2.80&Aring;" /> '''Crystal structure of...)
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[[Image:2imo.gif|left|200px]]<br /><applet load="2imo" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2imo, resolution 2.80&Aring;" />
 
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'''Crystal structure of allantoate amidohydrolase from Escherichia coli at pH 4.6'''<br />
 
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==Overview==
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==Crystal structure of allantoate amidohydrolase from Escherichia coli at pH 4.6==
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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.
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<StructureSection load='2imo' size='340' side='right'caption='[[2imo]]' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>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 [https://proteopedia.org/fgij/fg.htm?mol=2IMO FirstGlance]. <br>
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2IMO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IMO OCA].
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2imo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2imo OCA], [https://pdbe.org/2imo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2imo RCSB], [https://www.ebi.ac.uk/pdbsum/2imo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2imo ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/2imo TOPSAN]</span></td></tr>
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</table>
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==Reference==
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== Evolutionary Conservation ==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=17362992 17362992]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Escherichia coli]]
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Check<jmol>
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[[Category: Single protein]]
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<jmolCheckbox>
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[[Category: Agarwal, R.]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/im/2imo_consurf.spt"</scriptWhenChecked>
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[[Category: Burley, S.K.]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: NYSGXRC, New.York.Structural.GenomiX.Research.Consortium.]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: Swaminathan, S.]]
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</jmolCheckbox>
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[[Category: allantoate amidohydrolase]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2imo ConSurf].
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[[Category: allc]]
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<div style="clear:both"></div>
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[[Category: apoenzyme]]
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__TOC__
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[[Category: new york structural genomix research consortium]]
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</StructureSection>
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[[Category: nysgxrc]]
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[[Category: Large Structures]]
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[[Category: protein structure initiative]]
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[[Category: Agarwal R]]
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[[Category: psi-2]]
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[[Category: Burley SK]]
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[[Category: structural genomics]]
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[[Category: Swaminathan S]]
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[[Category: t1507]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:22:38 2007''
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Current revision

Crystal structure of allantoate amidohydrolase from Escherichia coli at pH 4.6

PDB ID 2imo

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