3tq0

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<StructureSection load='3tq0' size='340' side='right'caption='[[3tq0]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='3tq0' size='340' side='right'caption='[[3tq0]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3tq0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_major_mhom/il/81/friedlin Leishmania major mhom/il/81/friedlin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TQ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TQ0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3tq0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_major_strain_Friedlin Leishmania major strain Friedlin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TQ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TQ0 FirstGlance]. <br>
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</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=FUM:FUMARIC+ACID'>FUM</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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]] 1.9&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DHODH, lmjf16.0530, LMJF_16_0530 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=347515 Leishmania major MHOM/IL/81/Friedlin])</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=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=FUM:FUMARIC+ACID'>FUM</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dihydroorotate_oxidase_(fumarate) Dihydroorotate oxidase (fumarate)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.98.1 1.3.98.1] </span></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=3tq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tq0 OCA], [https://pdbe.org/3tq0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tq0 RCSB], [https://www.ebi.ac.uk/pdbsum/3tq0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tq0 ProSAT]</span></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=3tq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tq0 OCA], [https://pdbe.org/3tq0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tq0 RCSB], [https://www.ebi.ac.uk/pdbsum/3tq0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tq0 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q4QEW7_LEIMA Q4QEW7_LEIMA]
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Dihydroorotate dehydrogenase (DHODH) is the fourth enzyme in the de novo pyrimidine biosynthetic pathway and has been exploited as the target for therapy against proliferative and parasitic diseases. In this study, we report the crystal structures of DHODH from Leishmania major, the species of Leishmania associated with zoonotic cutaneous leishmaniasis, in its apo form and in complex with orotate and fumarate molecules. Both orotate and fumarate were found to bind to the same active site and exploit similar interactions, consistent with a ping-pong mechanism described for class 1A DHODHs. Analysis of LmDHODH structures reveals that rearrangements in the conformation of the catalytic loop have direct influence on the dimeric interface. This is the first structural evidence of a relationship between the dimeric form and the catalytic mechanism. According to our analysis, the high sequence and structural similarity observed among trypanosomatid DHODH suggest that a single strategy of structure-based inhibitor design can be used to validate DHODH as a druggable target against multiple neglected tropical diseases such as Leishmaniasis, Sleeping sickness and Chagas' diseases.
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Crystal structure of dihydroorotate dehydrogenase from Leishmania major.,Cordeiro AT, Feliciano PR, Pinheiro MP, Nonato MC Biochimie. 2012 Apr 21. PMID:22542640<ref>PMID:22542640</ref>
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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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<div class="pdbe-citations 3tq0" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Dihydroorotate dehydrogenase 3D structures|Dihydroorotate dehydrogenase 3D structures]]
*[[Dihydroorotate dehydrogenase 3D structures|Dihydroorotate dehydrogenase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Leishmania major mhom/il/81/friedlin]]
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[[Category: Leishmania major strain Friedlin]]
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[[Category: Cordeiro, A T]]
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[[Category: Cordeiro AT]]
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[[Category: Feliciano, P R]]
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[[Category: Feliciano PR]]
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[[Category: Nonato, M C]]
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[[Category: Nonato MC]]
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[[Category: Oxidoreductase]]
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Current revision

Crystal structure of Leishmania major dihydroorotate dehydrogenase in complex with fumarate

PDB ID 3tq0

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