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2q09

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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==
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<StructureSection load='2q09' size='340' side='right'caption='[[2q09]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
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<StructureSection load='2q09' size='340' side='right'caption='[[2q09]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<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>
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</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>
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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=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>
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<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>
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</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>
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<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&reg;/PubMed&reg;, 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/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Imidazolonepropionase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Miscellaneous nucleic acid]]
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[[Category: Burley SK]]
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[[Category: Burley, S K]]
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[[Category: Eswaramoorthy S]]
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[[Category: Eswaramoorthy, S]]
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[[Category: Swaminathan S]]
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[[Category: Structural genomic]]
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[[Category: Tyagi R]]
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[[Category: Swaminathan, S]]
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[[Category: Tyagi, R]]
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[[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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Revision as of 07:48, 9 March 2022

Crystal structure of Imidazolonepropionase from environmental sample with bound inhibitor 3-(2,5-Dioxo-imidazolidin-4-yl)-propionic acid

PDB ID 2q09

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