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3qw3

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==Structure of Leishmania donovani OMP decarboxylase==
==Structure of Leishmania donovani OMP decarboxylase==
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<StructureSection load='3qw3' size='340' side='right' caption='[[3qw3]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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<StructureSection load='3qw3' size='340' side='right'caption='[[3qw3]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qw3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Leishmania_infantum Leishmania infantum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QW3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QW3 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qw3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_infantum Leishmania infantum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QW3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QW3 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
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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]] 1.7&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LinJ16.0560 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5671 Leishmania infantum])</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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qw3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qw3 RCSB], [http://www.ebi.ac.uk/pdbsum/3qw3 PDBsum]</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=3qw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qw3 OCA], [https://pdbe.org/3qw3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qw3 RCSB], [https://www.ebi.ac.uk/pdbsum/3qw3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qw3 ProSAT]</span></td></tr>
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<table>
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</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/A4HWV2_LEIIN A4HWV2_LEIIN]
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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®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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==See Also==
==See Also==
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*[[Phosphoribosyltransferase|Phosphoribosyltransferase]]
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*[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]]
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== References ==
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*[[Uridine 5'-monophosphate synthase 3D structures|Uridine 5'-monophosphate synthase 3D structures]]
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Leishmania infantum]]
[[Category: Leishmania infantum]]
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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: Orotidine monophosphate decarboxylase]]
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[[Category: Transferase]]
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Current revision

Structure of Leishmania donovani OMP decarboxylase

PDB ID 3qw3

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