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3qw4

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Current revision (10:50, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3qw4' size='340' side='right'caption='[[3qw4]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='3qw4' size='340' side='right'caption='[[3qw4]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qw4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Leido Leido]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QW4 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qw4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_donovani Leishmania donovani]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QW4 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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=U5P:URIDINE-5-MONOPHOSPHATE'>U5P</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]] 3&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LDBPK_160560 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5661 LEIDO])</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=U5P:URIDINE-5-MONOPHOSPHATE'>U5P</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=3qw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qw4 OCA], [https://pdbe.org/3qw4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qw4 RCSB], [https://www.ebi.ac.uk/pdbsum/3qw4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qw4 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=3qw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qw4 OCA], [https://pdbe.org/3qw4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qw4 RCSB], [https://www.ebi.ac.uk/pdbsum/3qw4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qw4 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/H9ABT8_LEIDO H9ABT8_LEIDO]
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The final two steps of de novo uridine 5'-monophosphate (UMP) biosynthesis are catalyzed by orotate phosphoribosyltransferase (OPRT) and orotidine 5'-monophosphate decarboxylase (OMPDC). In most prokaryotes and simple eukaryotes these two enzymes are encoded by separate genes, whereas in mammals they are expressed as a bifunctional gene product called UMP synthase (UMPS), with OPRT at the N terminus and OMPDC at the C terminus. Leishmania and some closely related organisms also express a bifunctional enzyme for these two steps, but the domain order is reversed relative to mammalian UMPS. In this work we demonstrate that L. donovani UMPS (LdUMPS) is an essential enzyme in promastigotes and that it is sequestered in the parasite glycosome. We also present the crystal structure of the LdUMPS in complex with its product, UMP. This structure reveals an unusual tetramer with two head to head and two tail to tail interactions, resulting in two dimeric OMPDC and two dimeric OPRT functional domains. In addition, we provide structural and biochemical evidence that oligomerization of LdUMPS is controlled by product binding at the OPRT active site. We propose a model for the assembly of the catalytically relevant LdUMPS tetramer and discuss the implications for the structure of mammalian UMPS.
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The Leishmania donovani UMP synthase is essential for promastigote viability and has an unusual tetrameric structure that exhibits substrate-controlled oligomerization.,French JB, Yates PA, Soysa DR, Boitz JM, Carter NS, Chang B, Ullman B, Ealick SE J Biol Chem. 2011 Jun 10;286(23):20930-41. Epub 2011 Apr 19. PMID:21507942<ref>PMID:21507942</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 3qw4" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]]
*[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 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: Leido]]
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[[Category: Leishmania donovani]]
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[[Category: Ealick, S E]]
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[[Category: Ealick SE]]
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[[Category: French, J B]]
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[[Category: French JB]]
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[[Category: Lyase]]
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[[Category: N-terminal orotidine monophosphate decarboxylase domain c-terminal orotate phosphoribosyltransferase domain]]
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[[Category: Transferase]]
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Current revision

Structure of Leishmania donovani UMP synthase

PDB ID 3qw4

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