2q09: Difference between revisions

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New page: left|200px<br /><applet load="2q09" size="450" color="white" frame="true" align="right" spinBox="true" caption="2q09, resolution 1.97Å" /> '''Crystal structure of...
 
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[[Image:2q09.jpg|left|200px]]<br /><applet load="2q09" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2q09, resolution 1.97&Aring;" />
'''Crystal structure of Imidazolonepropionase from environmental sample with bound inhibitor 3-(2,5-Dioxo-imidazolidin-4-yl)-propionic acid'''<br />


==About this Structure==
==Crystal structure of Imidazolonepropionase from environmental sample with bound inhibitor 3-(2,5-Dioxo-imidazolidin-4-yl)-propionic acid==
2Q09 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with FE and DI6 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2Q09 OCA].  
<StructureSection load='2q09' size='340' side='right'caption='[[2q09]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
[[Category: ]]
== Structural highlights ==
[[Category: Imidazolonepropionase]]
<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>
[[Category: Protein complex]]
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.97&#8491;</td></tr>
[[Category: Burley, S.K.]]
<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>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
[[Category: Eswaramoorthy, S.]]
<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>
[[Category: NYSGXRC, New.York.Structural.GenomiX.Research.Consortium.]]
</table>
[[Category: Swaminathan, S.]]
== Evolutionary Conservation ==
[[Category: Tyagi, R.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: DI6]]
Check<jmol>
[[Category: FE]]
  <jmolCheckbox>
[[Category: 3-(2]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q0/2q09_consurf.spt"</scriptWhenChecked>
[[Category: 5-dioxo-imidazolidin-4yl)-propionic acid]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
[[Category: 9252h]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: imidazolonepropionase]]
  </jmolCheckbox>
[[Category: new york structural genomix research consortium]]
</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].
[[Category: nysgxrc]]
<div style="clear:both"></div>
[[Category: protein structure initiative]]
<div style="background-color:#fffaf0;">
[[Category: psi2_community]]
== Publication Abstract from PubMed ==
[[Category: structural genomics]]
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.


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:45:00 2007''
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>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2q09" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Burley SK]]
[[Category: Eswaramoorthy S]]
[[Category: Swaminathan S]]
[[Category: Tyagi R]]

Latest revision as of 08:31, 30 October 2024

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

2q09, resolution 1.97Å

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