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| - | ==CRYSTAL STRUCTURE OF F96S MUTANT OF PLASMODIUM FALCIPARUM TRIOSEPHOSPHATE ISOMERASE WITH 3-PHOSPHOGLYCERATE BOUND AT THE DIMER INTERFACE== | + | |
| - | <StructureSection load='2vfe' size='340' side='right' caption='[[2vfe]], [[Resolution|resolution]] 2.20Å' scene=''> | + | ==Crystal structure of F96S mutant of Plasmodium falciparum triosephosphate isomerase with 3- phosphoglycerate bound at the dimer interface== |
| | + | <StructureSection load='2vfe' size='340' side='right'caption='[[2vfe]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vfe]] 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=2VFE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VFE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vfe]] 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=2VFE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VFE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lzo|1lzo]], [[1m7p|1m7p]], [[1woa|1woa]], [[1wob|1wob]], [[1lyx|1lyx]], [[1m7o|1m7o]], [[1o5x|1o5x]], [[1vga|1vga]], [[1ydv|1ydv]], [[2vfd|2vfd]], [[2vff|2vff]], [[2vfg|2vfg]], [[2vfh|2vfh]], [[2vfi|2vfi]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </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=2vfe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vfe OCA], [https://pdbe.org/2vfe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vfe RCSB], [https://www.ebi.ac.uk/pdbsum/2vfe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vfe 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=2vfe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vfe OCA], [http://pdbe.org/2vfe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vfe RCSB], [http://www.ebi.ac.uk/pdbsum/2vfe PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/TPIS_PLAFA TPIS_PLAFA] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vf/2vfe_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vf/2vfe_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | ==See Also== | | ==See Also== |
| - | *[[Triose Phosphate Isomerase|Triose Phosphate Isomerase]] | + | *[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Plafa]] | + | [[Category: Large Structures]] |
| - | [[Category: Triose-phosphate isomerase]]
| + | |
| - | [[Category: Balaram, H]]
| + | |
| - | [[Category: Balaram, P]]
| + | |
| - | [[Category: Banerjee, M]]
| + | |
| - | [[Category: Gayathri, P]]
| + | |
| - | [[Category: Murthy, M R.N]]
| + | |
| - | [[Category: Vijayalakshmi, A]]
| + | |
| - | [[Category: 3-phosphoglycerate]]
| + | |
| - | [[Category: Dimer interface]]
| + | |
| - | [[Category: Fatty acid biosynthesis]]
| + | |
| - | [[Category: Gluconeogenesis]]
| + | |
| - | [[Category: Glycolysis]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Lipid synthesis]]
| + | |
| - | [[Category: Pentose shunt]]
| + | |
| | [[Category: Plasmodium falciparum]] | | [[Category: Plasmodium falciparum]] |
| - | [[Category: Triosephosphate isomerase]] | + | [[Category: Balaram H]] |
| | + | [[Category: Balaram P]] |
| | + | [[Category: Banerjee M]] |
| | + | [[Category: Gayathri P]] |
| | + | [[Category: Murthy MRN]] |
| | + | [[Category: Vijayalakshmi A]] |
| Structural highlights
Function
TPIS_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
Plasmodium falciparum TIM (PfTIM) is unique in possessing a Phe residue at position 96 in place of the conserved Ser that is found in TIMs from the majority of other organisms. In order to probe the role of residue 96, three PfTIM mutants, F96S, F96H and F96W, have been biochemically and structurally characterized. The three mutants exhibited reduced catalytic efficiency and a decrease in substrate-binding affinity, with the most pronounced effects being observed for F96S and F96H. The k(cat) values and K(m) values are (2.54 +/- 0.19) x 10(5) min(-1) and 0.39 +/- 0.049 mM, respectively, for the wild type; (3.72 +/- 0.28) x 10(3) min(-1) and 2.18 +/- 0.028 mM, respectively, for the F96S mutant; (1.11 +/- 0.03) x 10(4) min(-1) and 2.62 +/- 0.042 mM, respectively, for the F96H mutant; and (1.48 +/- 0.05) x 10(5) min(-1) and 1.20 +/- 0.056 mM, respectively, for the F96W mutant. Unliganded and 3-phosphoglycerate (3PG) complexed structures are reported for the wild-type enzyme and the mutants. The ligand binds to the active sites of the wild-type enzyme (wtPfTIM) and the F96W mutant, with a loop-open state in the former and both open and closed states in the latter. In contrast, no density for the ligand could be detected at the active sites of the F96S and F96H mutants under identical conditions. The decrease in ligand affinity could be a consequence of differences in the water network connecting residue 96 to Ser73 in the vicinity of the active site. Soaking of crystals of wtPfTIM and the F96S and F96H mutants resulted in the binding of 3PG at a dimer-interface site. In addition, loop closure at the liganded active site was observed for wtPfTIM. The dimer-interface site in PfTIM shows strong electrostatic anchoring of the phosphate group involving the Arg98 and Lys112 residues of PfTIM.
Biochemical and structural characterization of residue 96 mutants of Plasmodium falciparum triosephosphate isomerase: active-site loop conformation, hydration and identification of a dimer-interface ligand-binding site.,Gayathri P, Banerjee M, Vijayalakshmi A, Balaram H, Balaram P, Murthy MR Acta Crystallogr D Biol Crystallogr. 2009 Aug;65(Pt 8):847-57. Epub 2009, Jul 17. PMID:19622869[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gayathri P, Banerjee M, Vijayalakshmi A, Balaram H, Balaram P, Murthy MR. Biochemical and structural characterization of residue 96 mutants of Plasmodium falciparum triosephosphate isomerase: active-site loop conformation, hydration and identification of a dimer-interface ligand-binding site. Acta Crystallogr D Biol Crystallogr. 2009 Aug;65(Pt 8):847-57. Epub 2009, Jul 17. PMID:19622869 doi:10.1107/S0907444909018666
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