|
|
| (13 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| - | [[Image:2imo.gif|left|200px]] | |
| | | | |
| - | {{Structure
| + | ==Crystal structure of allantoate amidohydrolase from Escherichia coli at pH 4.6== |
| - | |PDB= 2imo |SIZE=350|CAPTION= <scene name='initialview01'>2imo</scene>, resolution 2.80Å
| + | <StructureSection load='2imo' size='340' side='right'caption='[[2imo]]' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
| + | <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> |
| - | |ACTIVITY=
| + | </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> |
| - | |GENE= allC_ecoli ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
| + | </table> |
| - | |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>
| + | == Evolutionary Conservation == |
| - | |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>
| + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | }}
| + | Check<jmol> |
| - | | + | <jmolCheckbox> |
| - | '''Crystal structure of allantoate amidohydrolase from Escherichia coli at pH 4.6'''
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/im/2imo_consurf.spt"</scriptWhenChecked> |
| - | | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | | + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | ==Overview== | + | </jmolCheckbox> |
| - | 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.
| + | </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]. |
| - | | + | <div style="clear:both"></div> |
| - | ==About this Structure==
| + | __TOC__ |
| - | 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].
| + | </StructureSection> |
| - | | + | [[Category: Large Structures]] |
| - | ==Reference== | + | [[Category: Agarwal R]] |
| - | 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: Burley SK]] |
| - | [[Category: Escherichia coli]] | + | [[Category: Swaminathan S]] |
| - | [[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]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 06:32:32 2008''
| + | |
