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| | <StructureSection load='2g9z' size='340' side='right'caption='[[2g9z]], [[Resolution|resolution]] 1.96Å' scene=''> | | <StructureSection load='2g9z' size='340' side='right'caption='[[2g9z]], [[Resolution|resolution]] 1.96Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2g9z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_11006_[[candida_stellatoidea]] Atcc 11006 [[candida stellatoidea]]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G9Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G9Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2g9z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G9Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G9Z FirstGlance]. <br> |
| - | </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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=VNP:3-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-5-(2-{[HYDROXY(PHOSPHONOAMINO)PHOSPHORYL]OXY}ETHYL)-4-METHYL-1,3-THIAZOL-3-IUM'>VNP</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]] 1.96Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ig0|1ig0]]</div></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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=VNP:3-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-5-(2-{[HYDROXY(PHOSPHONOAMINO)PHOSPHORYL]OXY}ETHYL)-4-METHYL-1,3-THIAZOL-3-IUM'>VNP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CA1462 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5476 ATCC 11006 [[Candida stellatoidea]]])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Thiamine_diphosphokinase Thiamine diphosphokinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.6.2 2.7.6.2] </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=2g9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g9z OCA], [https://pdbe.org/2g9z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g9z RCSB], [https://www.ebi.ac.uk/pdbsum/2g9z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g9z 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=2g9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g9z OCA], [https://pdbe.org/2g9z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g9z RCSB], [https://www.ebi.ac.uk/pdbsum/2g9z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g9z ProSAT]</span></td></tr> |
| | </table> | | </table> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Candida albicans]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thiamine diphosphokinase]]
| + | [[Category: Abergel C]] |
| - | [[Category: Abergel, C]] | + | [[Category: Claverie JM]] |
| - | [[Category: Claverie, J M]] | + | [[Category: Monchois V]] |
| - | [[Category: IGS-CNRS, France BIGSBacterial targets at]]
| + | [[Category: Rousselle T]] |
| - | [[Category: Monchois, V]] | + | [[Category: Santini S]] |
| - | [[Category: Rousselle, T]] | + | |
| - | [[Category: Santini, S]] | + | |
| - | [[Category: Bacterial targets at igs-cnr]]
| + | |
| - | [[Category: Big]]
| + | |
| - | [[Category: France]]
| + | |
| - | [[Category: Profun]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Thiamin pyrophosphokinase]]
| + | |
| - | [[Category: Thiamin-pnp]]
| + | |
| - | [[Category: Tpk]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
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
BACKGROUND: In search of new antifungal targets of potential interest for pharmaceutical companies, we initiated a comparative genomics study to identify the most promising protein-coding genes in fungal genomes. One criterion was the protein sequence conservation between reference pathogenic genomes. A second criterion was that the corresponding gene in Saccharomyces cerevisiae should be essential. Since thiamine pyrophosphate is an essential product involved in a variety of metabolic pathways, proteins responsible for its production satisfied these two criteria. RESULTS: We report the enzymatic characterization and the crystallographic structure of the Candida albicans Thiamine pyrophosphokinase. The protein was co-crystallized with thiamine or thiamine-PNP. CONCLUSION: The presence of an inorganic phosphate in the crystallographic structure opposite the known AMP binding site relative to the thiamine moiety suggests that a second AMP molecule could be accommodated in the C. albicans structure. Together with the crystallographic structures of the enzyme/substrate complexes this suggests the existence of a secondary, less specific, nucleotide binding site in the Candida albicans thiamine pyrophosphokinase which could transiently serve during the release or the binding of ATP. The structures also highlight a conserved Glutamine residue (Q138) which could interact with the ATP alpha-phosphate and act as gatekeeper. Finally, the TPK/Thiamine-PNP complex is consistent with a one step mechanism of pyrophosphorylation.
Structural characterization of CA1462, the Candida albicans thiamine pyrophosphokinase.,Santini S, Monchois V, Mouz N, Sigoillot C, Rousselle T, Claverie JM, Abergel C BMC Struct Biol. 2008 Jul 24;8:33. PMID:18652651[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Santini S, Monchois V, Mouz N, Sigoillot C, Rousselle T, Claverie JM, Abergel C. Structural characterization of CA1462, the Candida albicans thiamine pyrophosphokinase. BMC Struct Biol. 2008 Jul 24;8:33. PMID:18652651 doi:http://dx.doi.org/10.1186/1472-6807-8-33
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