4yxg: Difference between revisions
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==F96Y Mutant of Plasmodium Falciparum Triosephosphate Isomerase== | ==F96Y Mutant of Plasmodium Falciparum Triosephosphate Isomerase== | ||
<StructureSection load='4yxg' size='340' side='right' caption='[[4yxg]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='4yxg' size='340' side='right'caption='[[4yxg]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4yxg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YXG OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4yxg]] 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=4YXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YXG FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></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=4yxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yxg OCA], [https://pdbe.org/4yxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yxg RCSB], [https://www.ebi.ac.uk/pdbsum/4yxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yxg ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/TPIS_PLAFA TPIS_PLAFA] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 4yxg" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4yxg" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Plasmodium falciparum]] | ||
[[Category: | [[Category: Balaram P]] | ||
[[Category: | [[Category: Murthy MRN]] | ||
[[Category: | [[Category: Pareek V]] | ||
Latest revision as of 18:40, 8 November 2023
F96Y Mutant of Plasmodium Falciparum Triosephosphate IsomeraseF96Y Mutant of Plasmodium Falciparum Triosephosphate Isomerase
Structural highlights
FunctionPublication Abstract from PubMedDespite extensive research on triosephosphate isomerase (TIM), there exists a gap in understanding the remarkable conjunction between catalytic loop-6 (residue 166-176) movement and conformational flip of Glu165 (catalytic base) upon substrate binding, thus priming the active site for efficient catalysis. The overwhelming occurrence of Ser at position 96 (98% of the 6277 unique TIM sequences), spatially proximal to E165 and the loop-6 residues, raises questions about its role in catalysis. Notably, Plasmodium falciparum TIM has an extremely rare residue, Phe, at this position and curiously, the mutant F96S was catalytically defective. We provide insights into the influence of residue 96 on the loop-6 dynamics and E165 positioning by combining the kinetic and structural studies on the PfTIM F96 mutants, F96Y, F96A, F96S/S73A and F96S/L167V with sequence conservation analysis and comparative analysis of the available apo and holo structures of the enzyme from diverse organisms. Connecting active site loop conformations and catalysis in triosephosphate isomerase: insights from a rare variation at residue 96 in the plasmodial enzyme.,Pareek V, Samanta M, Joshi NV, Balaram H, Murthy MR, Balaram P Chembiochem. 2016 Jan 14. doi: 10.1002/cbic.201500532. PMID:26762569[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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