2q09

<StructureSection load='2q09' size='340' side='right'caption='[[2q09]], [[Resolution|resolution]] 1.97&Aring;' scene=''>

<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>

</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>

<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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== Publication Abstract from PubMed ==

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.

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>

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<div class="pdbe-citations 2q09" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Imidazolonepropionase]]

[[Category: Burley, S K]]

[[Category: Eswaramoorthy, S]]

[[Category: Structural genomic]]

[[Category: Swaminathan, S]]

[[Category: Tyagi, R]]

[[Category: Psi-2 community]]