2vun

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[[Image:2vun.png|left|200px]]
 
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{{STRUCTURE_2vun| PDB=2vun | SCENE= }}
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==The Crystal Structure of Enamidase at 1.9 A Resolution - A new Member of the Amidohydrolase Superfamily==
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<StructureSection load='2vun' size='340' side='right'caption='[[2vun]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2vun]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Eubacterium_barkeri Eubacterium barkeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VUN FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.89&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vun OCA], [https://pdbe.org/2vun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vun RCSB], [https://www.ebi.ac.uk/pdbsum/2vun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vun ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ENA_EUBBA ENA_EUBBA] Decyclization of 6-oxo-1,4,5,6-tetrahydronicotinate to form 2-(enamine)glutarate, followed by hydrolysis to form (S)-2-formylglutarate.<ref>PMID:16894175</ref> <ref>PMID:18805424</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vu/2vun_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2vun ConSurf].
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<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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The hydrolysis of 1,4,5,6-tetrahydro-6-oxonicotinate to 2-formylglutarate is a central step in the catabolism of nicotinate in several Clostridia and Proteobacteria. This reaction is catalyzed by the novel enzyme enamidase, a new member of the amidohydrolase superfamily as indicated by its unique reaction, sequence relationship, and the stoichiometric binding of iron and zinc. A hallmark of enamidase is its capability to catalyze a two-step reaction: the initial decyclization of 1,4,5,6-tetrahydro-6-oxonicotinate leading to 2-(enamine)glutarate followed by an additional hydrolysis step yielding (S)-2-formylglutarate. Here, we present the crystal structure of enamidase from Eubacterium barkeri at 1.9 A resolution, providing a structural basis for catalysis and suggesting a mechanism for its exceptional activity and enantioselectivity. The enzyme forms a 222-symmetric tetramer built up by a dimer of dimers. Each enamidase monomer consists of a composite beta-sandwich domain and an (alpha/beta)(8)-TIM-barrel domain harboring the active site. With its catalytic binuclear metal center comprising both zinc and iron ions, enamidase represents a special case of subtype II amidohydrolases.
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===THE CRYSTAL STRUCTURE OF ENAMIDASE AT 1.9 A RESOLUTION - A NEW MEMBER OF THE AMIDOHYDROLASE SUPERFAMILY===
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The crystal structure of enamidase: a bifunctional enzyme of the nicotinate catabolism.,Kress D, Alhapel A, Pierik AJ, Essen LO J Mol Biol. 2008 Dec 26;384(4):837-47. Epub 2008 Sep 12. PMID:18805424<ref>PMID:18805424</ref>
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{{ABSTRACT_PUBMED_18805424}}
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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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==About this Structure==
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<div class="pdbe-citations 2vun" style="background-color:#fffaf0;"></div>
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[[2vun]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Eubacterium_barkeri Eubacterium barkeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VUN OCA].
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== References ==
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[[Category: Enamidase]]
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<references/>
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__TOC__
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</StructureSection>
[[Category: Eubacterium barkeri]]
[[Category: Eubacterium barkeri]]
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[[Category: Alhapel, A.]]
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[[Category: Large Structures]]
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[[Category: Essen, L O.]]
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[[Category: Alhapel A]]
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[[Category: Kress, D.]]
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[[Category: Essen L-O]]
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[[Category: Pierik, A J.]]
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[[Category: Kress D]]
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[[Category: Amidohydrolase]]
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[[Category: Pierik AJ]]
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[[Category: Binuclear metal center]]
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[[Category: Hydrolase]]
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[[Category: Nicotinate degradation]]
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[[Category: Stereospecificity]]
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Current revision

The Crystal Structure of Enamidase at 1.9 A Resolution - A new Member of the Amidohydrolase Superfamily

PDB ID 2vun

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