|
|
| Line 1: |
Line 1: |
|
| |
|
| ==Crystal structure of allantoate amidohydrolase from Escherichia coli at pH 4.6== | | ==Crystal structure of allantoate amidohydrolase from Escherichia coli at pH 4.6== |
| <StructureSection load='2imo' size='340' side='right' caption='[[2imo]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='2imo' size='340' side='right'caption='[[2imo]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <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> | | <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> |
| </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> | | </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> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1z2l|1z2l]]</td></tr>
| |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">allC_ecoli ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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> | |
| </table> | | </table> |
| == 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>
| |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 21: |
Line 16: |
| </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]. | | </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> | | <div style="clear:both"></div> |
| <div style="background-color:#fffaf0;">
| |
| == 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®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| |
| </div>
| |
| <div class="pdbe-citations 2imo" style="background-color:#fffaf0;"></div>
| |
| == References ==
| |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Ecoli]] | | [[Category: Large Structures]] |
| [[Category: Agarwal, R]] | | [[Category: Agarwal R]] |
| [[Category: Burley, S K]] | | [[Category: Burley SK]] |
| [[Category: Structural genomic]]
| | [[Category: Swaminathan S]] |
| [[Category: Swaminathan, S]] | |
| [[Category: Allantoate amidohydrolase]]
| |
| [[Category: Allc]]
| |
| [[Category: Apoenzyme]]
| |
| [[Category: Hydrolase]]
| |
| [[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]]
| |
| [[Category: PSI, Protein structure initiative]]
| |
| [[Category: T1507]]
| |
