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[[Image:1f76.jpg|left|200px]]
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{{STRUCTURE_1f76|  PDB=1f76  |  SCENE=  }}
'''ESCHERICHIA COLI DIHYDROOROTATE DEHYDROGENASE'''


==ESCHERICHIA COLI DIHYDROOROTATE DEHYDROGENASE==
<StructureSection load='1f76' size='340' side='right'caption='[[1f76]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1f76]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F76 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F76 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=ORO:OROTIC+ACID'>ORO</scene></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=1f76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f76 OCA], [https://pdbe.org/1f76 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f76 RCSB], [https://www.ebi.ac.uk/pdbsum/1f76 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f76 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PYRD_ECOLI PYRD_ECOLI] Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.<ref>PMID:10074342</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/f7/1f76_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1f76 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The flavoenzymes dihydroorotate dehydrogenases (DHODs) catalyze the fourth and only redox step in the de novo biosynthesis of UMP. Enzymes belonging to class 2, according to their amino acid sequence, are characterized by having a serine residue as the catalytic base and a longer N terminus. The structure of class 2 E. coli DHOD, determined by MAD phasing, showed that the N-terminal extension forms a separate domain. The catalytic serine residue has an environment differing from the equivalent cysteine in class 1 DHODs. Significant differences between the two classes of DHODs were identified by comparison of the E. coli DHOD with the other known DHOD structures, and differences with the class 2 human DHOD explain the variation in their inhibitors.


==Overview==
E. coli dihydroorotate dehydrogenase reveals structural and functional distinctions between different classes of dihydroorotate dehydrogenases.,Norager S, Jensen KF, Bjornberg O, Larsen S Structure. 2002 Sep;10(9):1211-23. PMID:12220493<ref>PMID:12220493</ref>
The flavoenzymes dihydroorotate dehydrogenases (DHODs) catalyze the fourth and only redox step in the de novo biosynthesis of UMP. Enzymes belonging to class 2, according to their amino acid sequence, are characterized by having a serine residue as the catalytic base and a longer N terminus. The structure of class 2 E. coli DHOD, determined by MAD phasing, showed that the N-terminal extension forms a separate domain. The catalytic serine residue has an environment differing from the equivalent cysteine in class 1 DHODs. Significant differences between the two classes of DHODs were identified by comparison of the E. coli DHOD with the other known DHOD structures, and differences with the class 2 human DHOD explain the variation in their inhibitors.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1F76 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F76 OCA].
</div>
<div class="pdbe-citations 1f76" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
E. coli dihydroorotate dehydrogenase reveals structural and functional distinctions between different classes of dihydroorotate dehydrogenases., Norager S, Jensen KF, Bjornberg O, Larsen S, Structure. 2002 Sep;10(9):1211-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12220493 12220493]
*[[Dihydroorotate dehydrogenase 3D structures|Dihydroorotate dehydrogenase 3D structures]]
[[Category: Dihydroorotate oxidase]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Bjornberg, O.]]
__TOC__
[[Category: Jensen, K F.]]
</StructureSection>
[[Category: Larsen, S.]]
[[Category: Escherichia coli K-12]]
[[Category: Norager, S.]]
[[Category: Large Structures]]
[[Category: Alpha-beta-barrel]]
[[Category: Bjornberg O]]
[[Category: Fmn binding domain]]
[[Category: Jensen KF]]
[[Category: Monomer]]
[[Category: Larsen S]]
[[Category: Orotate complex]]
[[Category: Norager S]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:59:07 2008''
Retrieved from "https://proteopedia.org/1f76"