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| ==Crystal structure of Imidazolonepropionase from environmental sample with bound inhibitor 3-(2,5-Dioxo-imidazolidin-4-yl)-propionic acid== | | ==Crystal structure of Imidazolonepropionase from environmental sample with bound inhibitor 3-(2,5-Dioxo-imidazolidin-4-yl)-propionic acid== |
| <StructureSection load='2q09' size='340' side='right'caption='[[2q09]], [[Resolution|resolution]] 1.97Å' scene=''> | | <StructureSection load='2q09' size='340' side='right'caption='[[2q09]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[2q09]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Miscellaneous_nucleic_acid Miscellaneous nucleic acid]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q09 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2Q09 FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q09 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DI6:3-[(4S)-2,5-DIOXOIMIDAZOLIDIN-4-YL]PROPANOIC+ACID'>DI6</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</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=2q09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q09 OCA], [https://pdbe.org/2q09 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q09 RCSB], [https://www.ebi.ac.uk/pdbsum/2q09 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q09 ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/2q09 TOPSAN]</span></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>
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| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gok|2gok]], [[2oof|2oof]], [[2puz|2puz]]</td></tr>
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| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Imidazolonepropionase Imidazolonepropionase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.7 3.5.2.7] </span></td></tr>
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| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2q09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q09 OCA], [http://pdbe.org/2q09 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2q09 RCSB], [http://www.ebi.ac.uk/pdbsum/2q09 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2q09 ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/2q09 TOPSAN]</span></td></tr> | |
| </table> | | </table> |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
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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=2q09 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=2q09 ConSurf]. |
| <div style="clear:both"></div> | | <div style="clear:both"></div> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Imidazolonepropionase (HutI) (imidazolone-5-propanote hydrolase, EC 3.5.2.7) is a member of the amidohydrolase superfamily and catalyzes the conversion of imidazolone-5-propanoate to N-formimino-L-glutamate in the histidine degradation pathway. We have determined the three-dimensional crystal structures of HutI from Agrobacterium tumefaciens (At-HutI) and an environmental sample from the Sargasso Sea Ocean Going Survey (Es-HutI) bound to the product [ N-formimino-L-glutamate (NIG)] and an inhibitor [3-(2,5-dioxoimidazolidin-4-yl)propionic acid (DIP)], respectively. In both structures, the active site is contained within each monomer, and its organization displays the landmark feature of the amidohydrolase superfamily, showing a metal ligand (iron), four histidines, and one aspartic acid. A catalytic mechanism involving His265 is proposed on the basis of the inhibitor-bound structure. This mechanism is applicable to all HutI forms.
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| A common catalytic mechanism for proteins of the HutI family.,Tyagi R, Eswaramoorthy S, Burley SK, Raushel FM, Swaminathan S Biochemistry. 2008 May 20;47(20):5608-15. Epub 2008 Apr 29. PMID:18442260<ref>PMID:18442260</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 2q09" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Imidazolonepropionase]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Miscellaneous nucleic acid]]
| | [[Category: Burley SK]] |
| [[Category: Burley, S K]] | | [[Category: Eswaramoorthy S]] |
| [[Category: Eswaramoorthy, S]] | | [[Category: Swaminathan S]] |
| [[Category: Structural genomic]]
| | [[Category: Tyagi R]] |
| [[Category: Swaminathan, S]] | |
| [[Category: Tyagi, R]] | |
| [[Category: Hydrolase]]
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| [[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]]
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| [[Category: PSI, Protein structure initiative]]
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| [[Category: Psi-2 community]]
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