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| | ==X-ray structure dihydrofolate reductase/thymidylate synthase from babesia bovis at 2.35A resolution== | | ==X-ray structure dihydrofolate reductase/thymidylate synthase from babesia bovis at 2.35A resolution== |
| - | <StructureSection load='3i3r' size='340' side='right' caption='[[3i3r]], [[Resolution|resolution]] 2.35Å' scene=''> | + | <StructureSection load='3i3r' size='340' side='right'caption='[[3i3r]], [[Resolution|resolution]] 2.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3i3r]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Babesia_bovis_t2bo Babesia bovis t2bo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I3R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3I3R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3i3r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Babesia_bovis_T2Bo Babesia bovis T2Bo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I3R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3I3R FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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]] 2.35Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BBOV_II000780 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=484906 Babesia bovis T2Bo])</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></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thymidylate_synthase Thymidylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.45 2.1.1.45] </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=3i3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i3r OCA], [https://pdbe.org/3i3r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3i3r RCSB], [https://www.ebi.ac.uk/pdbsum/3i3r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3i3r ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3i3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i3r OCA], [http://pdbe.org/3i3r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3i3r RCSB], [http://www.ebi.ac.uk/pdbsum/3i3r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3i3r ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A7ASX7_BABBO A7ASX7_BABBO]] Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism (By similarity).[PIRNR:PIRNR000389] | + | [https://www.uniprot.org/uniprot/A7ASX7_BABBO A7ASX7_BABBO] Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism (By similarity).[PIRNR:PIRNR000389] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 3i3r" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 3i3r" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Dihydrofolate reductase 3D structures|Dihydrofolate reductase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Babesia bovis t2bo]] | + | [[Category: Babesia bovis T2Bo]] |
| - | [[Category: Thymidylate synthase]] | + | [[Category: Large Structures]] |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Babesia bovi]]
| + | |
| - | [[Category: Dihydrofolate reductase]]
| + | |
| - | [[Category: Methyltransferase]]
| + | |
| - | [[Category: Ssgcid]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
A7ASX7_BABBO Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism (By similarity).[PIRNR:PIRNR000389]
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
Babesiosis is a tick-borne disease caused by eukaryotic Babesia parasites which are morphologically similar to Plasmodium falciparum, the causative agent of malaria in humans. Like Plasmodium, different species of Babesia are tuned to infect different mammalian hosts, including rats, dogs, horses and cattle. Most species of Plasmodium and Babesia possess an essential bifunctional enzyme for nucleotide synthesis and folate metabolism: dihydrofolate reductase-thymidylate synthase. Although thymidylate synthase is highly conserved across organisms, the bifunctional form of this enzyme is relatively uncommon in nature. The structural characterization of dihydrofolate reductase-thymidylate synthase in Babesia bovis, the causative agent of babesiosis in livestock cattle, is reported here. The apo state is compared with structures that contain dUMP, NADP and two different antifolate inhibitors: pemetrexed and raltitrexed. The complexes reveal modes of binding similar to that seen in drug-resistant malaria strains and point to the utility of applying structural studies with proven cancer chemotherapies towards infectious disease research.
Inhibitor-bound complexes of dihydrofolate reductase-thymidylate synthase from Babesia bovis.,Begley DW, Edwards TE, Raymond AC, Smith ER, Hartley RC, Abendroth J, Sankaran B, Lorimer DD, Myler PJ, Staker BL, Stewart LJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt, 9):1070-7. Epub 2011 Aug 16. PMID:21904052[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Begley DW, Edwards TE, Raymond AC, Smith ER, Hartley RC, Abendroth J, Sankaran B, Lorimer DD, Myler PJ, Staker BL, Stewart LJ. Inhibitor-bound complexes of dihydrofolate reductase-thymidylate synthase from Babesia bovis. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt, 9):1070-7. Epub 2011 Aug 16. PMID:21904052 doi:10.1107/S1744309111029009
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