View source for 6aj5


==Crystal structure of ligand-free type DHODH from Eimeria tenella==
<StructureSection load='6aj5' size='340' side='right'caption='[[6aj5]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6aj5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Eimeria_tenella Eimeria tenella]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AJ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AJ5 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]] 3.5&#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=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=6aj5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aj5 OCA], [https://pdbe.org/6aj5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6aj5 RCSB], [https://www.ebi.ac.uk/pdbsum/6aj5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6aj5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/U6KL66_EIMTE U6KL66_EIMTE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Dihydroorotate dehydrogenase (DHODH) is a mitochondrial monotopic membrane protein that plays an essential role in the pyrimidine de novo biosynthesis and electron transport chain pathways. In Eimeria tenella, an intracellular apicomplexan parasite that causes the most severe form of chicken coccidiosis, the activity of pyrimidine salvage pathway at the intracellular stage is negligible and it relies on the pyrimidine de novo biosynthesis pathway. Therefore, the enzymes of the de novo pathway are considered potential drug target candidates for the design of compounds with activity against this parasite. Although, DHODHs from E. tenella (EtDHODH), Plasmodium falciparum (PfDHODH), and human (HsDHODH) show distinct sensitivities to classical DHODH inhibitors, in this paper, we identify ferulenol as a potent inhibitor of both EtDHODH and HsDHODH. Additionally, we report the crystal structures of EtDHODH and HsDHODH in the absence and presence of ferulenol. Comparison of these enzymes showed that despite similar overall structures, the EtDHODH has a long insertion in the N-terminal helix region that assumes a disordered configuration. In addition, the crystal structures revealed that the ferulenol binding pocket of EtDHODH is larger than that of HsDHODH. These differences can be explored to accelerate structure-based design of inhibitors specifically targeting EtDHODH.

Structural and Biochemical Features of Eimeria tenella Dihydroorotate Dehydrogenase, a Potential Drug Target.,Sato D, Hartuti ED, Inaoka DK, Sakura T, Amalia E, Nagahama M, Yoshioka Y, Tsuji N, Nozaki T, Kita K, Harada S, Matsubayashi M, Shiba T Genes (Basel). 2020 Dec 7;11(12). pii: genes11121468. doi: 10.3390/genes11121468. PMID:33297567<ref>PMID:33297567</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6aj5" style="background-color:#fffaf0;"></div>

==See Also==
*[[Dihydroorotate dehydrogenase 3D structures|Dihydroorotate dehydrogenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Eimeria tenella]]
[[Category: Large Structures]]
[[Category: Amalia E]]
[[Category: Balogun EO]]
[[Category: Harada S]]
[[Category: Hartuti ED]]
[[Category: Inaoka DK]]
[[Category: Kita K]]
[[Category: Matsubayashi M]]
[[Category: Nagahama M]]
[[Category: Sato D]]
[[Category: Shiba T]]
[[Category: Tsuji N]]
[[Category: Yoshioka Y]]