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| | <StructureSection load='2zcg' size='340' side='right'caption='[[2zcg]], [[Resolution|resolution]] 2.22Å' scene=''> | | <StructureSection load='2zcg' size='340' side='right'caption='[[2zcg]], [[Resolution|resolution]] 2.22Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2zcg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Plafa Plafa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZCG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2ZCG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2zcg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZCG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZCG FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Orotidine-5'-phosphate_decarboxylase Orotidine-5'-phosphate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.23 4.1.1.23] </span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.223Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2zcg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zcg OCA], [http://pdbe.org/2zcg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zcg RCSB], [http://www.ebi.ac.uk/pdbsum/2zcg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zcg 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=2zcg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zcg OCA], [https://pdbe.org/2zcg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zcg RCSB], [https://www.ebi.ac.uk/pdbsum/2zcg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zcg ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8T6J6_PLAFA Q8T6J6_PLAFA] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Orotidine-5'-phosphate decarboxylase]] | + | [[Category: Plasmodium falciparum]] |
| - | [[Category: Plafa]]
| + | [[Category: Christopherson RI]] |
| - | [[Category: Christopherson, R I]] | + | [[Category: Guss JM]] |
| - | [[Category: Guss, J M]] | + | [[Category: Langley DB]] |
| - | [[Category: Langley, D B]] | + | [[Category: Shojaei M]] |
| - | [[Category: Shojaei, M]] | + | |
| - | [[Category: Decarboxylase]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Pyrimidine biosynthesis]]
| + | |
| - | [[Category: Tim barrel]]
| + | |
| Structural highlights
Function
Q8T6J6_PLAFA
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Orotidine 5'-monophosphate (OMP) decarboxylase from Plasmodium falciparum ( PfODCase, EC 4.1.1.23) has been overexpressed, purified, subjected to kinetic and biochemical analysis, and crystallized. The native enzyme is a homodimer with a subunit molecular mass of 38 kDa. The saturation curve for OMP as a substrate conformed to Michaelis-Menten kinetics with K m = 350 +/- 60 nM and V max = 2.70 +/- 0.10 micromol/min/mg protein. Inhibition patterns for nucleoside 5'-monophosphate analogues were linear competitive with respect to OMP with a decreasing potency of inhibition of PfODCase in the order: pyrazofurin 5'-monophosphate ( K i = 3.6 +/- 0.7 nM) > xanthosine 5'-monophosphate (XMP, K i = 4.4 +/- 0.7 nM) > 6-azauridine 5'-monophosphate (AzaUMP, K i = 12 +/- 3 nM) > allopurinol-3-riboside 5'-monophosphate ( K i = 240 +/- 20 nM). XMP is an approximately 150-fold more potent inhibitor of PfODCase compared with the human enzyme. The structure of PfODCase was solved in the absence of ligand and displays a classic TIM-barrel fold characteristic of the enzyme. Both the phosphate-binding loop and the betaalpha5-loop have conformational flexibility, which may be associated with substrate capture and product release along the reaction pathway.
Structure and Inhibition of Orotidine 5'-Monophosphate Decarboxylase from Plasmodium falciparum.,Langley DB, Shojaei M, Chan C, Lok HC, Mackay JP, Traut TW, Guss JM, Christopherson RI Biochemistry. 2008 Feb 28;. PMID:18303855[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Langley DB, Shojaei M, Chan C, Lok HC, Mackay JP, Traut TW, Guss JM, Christopherson RI. Structure and Inhibition of Orotidine 5'-Monophosphate Decarboxylase from Plasmodium falciparum. Biochemistry. 2008 Feb 28;. PMID:18303855 doi:10.1021/bi702390k
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