2vun: Difference between revisions

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{{Seed}}
[[Image:2vun.jpg|left|200px]]


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==The Crystal Structure of Enamidase at 1.9 A Resolution - A new Member of the Amidohydrolase Superfamily==
The line below this paragraph, containing "STRUCTURE_2vun", creates the "Structure Box" on the page.
<StructureSection load='2vun' size='340' side='right'caption='[[2vun]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
{{STRUCTURE_2vun|  PDB=2vun  |  SCENE=  }}
<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>
</table>
== Function ==
[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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vu/2vun_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


===THE CRYSTAL STRUCTURE OF ENAMIDASE AT 1.9 A RESOLUTION - A NEW MEMBER OF THE AMIDOHYDROLASE SUPERFAMILY===
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>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_18805424}}, adds the Publication Abstract to the page
<div class="pdbe-citations 2vun" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 18805424 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_18805424}}
__TOC__
 
</StructureSection>
==About this Structure==
2VUN is a 4 chains structure of sequences 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].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/18805424 18805424]
[[Category: Enamidase]]
[[Category: Eubacterium barkeri]]
[[Category: Eubacterium barkeri]]
[[Category: Alhapel, A.]]
[[Category: Large Structures]]
[[Category: Essen, L O.]]
[[Category: Alhapel A]]
[[Category: Kress, D.]]
[[Category: Essen L-O]]
[[Category: Pierik, A J.]]
[[Category: Kress D]]
[[Category: Amidohydrolase]]
[[Category: Pierik AJ]]
[[Category: Binuclear metal center]]
[[Category: Hydrolase]]
[[Category: Nicotinate degradation]]
[[Category: Stereospecificity]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 10 14:54:48 2008''
Retrieved from "https://proteopedia.org/2vun"