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==Structure of C126S mutant of Saccharomyces cerevisiae triosephosphate isomerase== | |||
=== | <StructureSection load='4ff7' size='340' side='right' caption='[[4ff7]], [[Resolution|resolution]] 1.86Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ff7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FF7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FF7 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ypi|1ypi]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TPI1, YDR050C, YD9609.05C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ff7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ff7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ff7 RCSB], [http://www.ebi.ac.uk/pdbsum/4ff7 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
All the members of the triosephosphate isomerase (TIM) family possess a cystein residue (Cys126) located near the catalytically essential Glu165. The evolutionarily conserved Cys126, however, does not seem to play a significant role in the catalytic activity. On the other hand, substitution of this residue by other amino acid residues destabilizes the dimeric enzyme, especially when Cys is replaced by Ser. In trying to assess the origin of this destabilization we have determined the crystal structure of Saccharomyces cerevisiae TIM (ScTIM) at 1.86 A resolution in the presence of PGA, which is only bound to one subunit. Comparisons of the wild type and mutant structures reveal that a change in the orientation of the Ser hydroxyl group, with respect to the Cys sulfhydryl group, leads to penetration of water molecules and apparent destabilization of residues 132-138. The latter results were confirmed by means of Molecular Dynamics, which showed that this region, in the mutated enzyme, collapses at about 70 ns. | |||
Effects of a buried cysteine-to-serine mutation on yeast triosephosphate isomerase structure and stability.,Hernandez-Santoyo A, Dominguez-Ramirez L, Reyes-Lopez CA, Gonzalez-Mondragon E, Hernandez-Arana A, Rodriguez-Romero A Int J Mol Sci. 2012;13(8):10010-21. doi: 10.3390/ijms130810010. Epub 2012 Aug 10. PMID:22949845<ref>PMID:22949845</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Triose Phosphate Isomerase|Triose Phosphate Isomerase]] | *[[Triose Phosphate Isomerase|Triose Phosphate Isomerase]] | ||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Saccharomyces cerevisiae s288c]] | [[Category: Saccharomyces cerevisiae s288c]] | ||
[[Category: Triose-phosphate isomerase]] | [[Category: Triose-phosphate isomerase]] | ||
[[Category: Hernandez-Santoyo, A | [[Category: Hernandez-Santoyo, A]] | ||
[[Category: Rodriguez-Romero, A | [[Category: Rodriguez-Romero, A]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
Revision as of 14:02, 21 December 2014
Structure of C126S mutant of Saccharomyces cerevisiae triosephosphate isomeraseStructure of C126S mutant of Saccharomyces cerevisiae triosephosphate isomerase
Structural highlights
Publication Abstract from PubMedAll the members of the triosephosphate isomerase (TIM) family possess a cystein residue (Cys126) located near the catalytically essential Glu165. The evolutionarily conserved Cys126, however, does not seem to play a significant role in the catalytic activity. On the other hand, substitution of this residue by other amino acid residues destabilizes the dimeric enzyme, especially when Cys is replaced by Ser. In trying to assess the origin of this destabilization we have determined the crystal structure of Saccharomyces cerevisiae TIM (ScTIM) at 1.86 A resolution in the presence of PGA, which is only bound to one subunit. Comparisons of the wild type and mutant structures reveal that a change in the orientation of the Ser hydroxyl group, with respect to the Cys sulfhydryl group, leads to penetration of water molecules and apparent destabilization of residues 132-138. The latter results were confirmed by means of Molecular Dynamics, which showed that this region, in the mutated enzyme, collapses at about 70 ns. Effects of a buried cysteine-to-serine mutation on yeast triosephosphate isomerase structure and stability.,Hernandez-Santoyo A, Dominguez-Ramirez L, Reyes-Lopez CA, Gonzalez-Mondragon E, Hernandez-Arana A, Rodriguez-Romero A Int J Mol Sci. 2012;13(8):10010-21. doi: 10.3390/ijms130810010. Epub 2012 Aug 10. PMID:22949845[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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