5eyw: Difference between revisions
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==Crystal structure of Litopenaeus vannamei triosephosphate isomerase complexed with 2-Phosphoglycolic acid== | ==Crystal structure of Litopenaeus vannamei triosephosphate isomerase complexed with 2-Phosphoglycolic acid== | ||
<StructureSection load='5eyw' size='340' side='right' caption='[[5eyw]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='5eyw' size='340' side='right'caption='[[5eyw]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5eyw]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EYW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EYW FirstGlance]. <br> | <table><tr><td colspan='2'>[[5eyw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Litopenaeus_vannamei Litopenaeus vannamei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EYW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EYW FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TIM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6689 Litopenaeus vannamei])</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='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=5eyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eyw OCA], [http://pdbe.org/5eyw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5eyw RCSB], [http://www.ebi.ac.uk/pdbsum/5eyw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5eyw 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=5eyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eyw OCA], [http://pdbe.org/5eyw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5eyw RCSB], [http://www.ebi.ac.uk/pdbsum/5eyw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5eyw ProSAT]</span></td></tr> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Litopenaeus vannamei]] | |||
[[Category: Triose-phosphate isomerase]] | [[Category: Triose-phosphate isomerase]] | ||
[[Category: Brieba, L G]] | [[Category: Brieba, L G]] | ||
Revision as of 11:03, 8 January 2020
Crystal structure of Litopenaeus vannamei triosephosphate isomerase complexed with 2-Phosphoglycolic acidCrystal structure of Litopenaeus vannamei triosephosphate isomerase complexed with 2-Phosphoglycolic acid
Structural highlights
Publication Abstract from PubMedTriosephosphate isomerase (TIM; EC 5.3.1.1) is a key enzyme involved in glycolysis and gluconeogenesis. Glycolysis is one of the most regulated metabolic pathways, however little is known about the structural mechanisms for its regulation in non-model organisms, like crustaceans. To understand the structure and function of this enzyme in invertebrates, we obtained the crystal structure of triosephosphate isomerase from the marine Pacific whiteleg shrimp (Litopenaeus vannamei, LvTIM) in complex with its inhibitor 2-phosphogyceric acid (2-PG) at 1.7A resolution. LvTIM assembles as a homodimer with residues 166-176 covering the active site and residue Glu166 interacting with the inhibitor. We found that LvTIM is the least stable TIM characterized to date, with the lowest range of melting temperatures, and with the lowest activation enthalpy associated with the thermal unfolding process reported. In TIMs dimer stabilization is maintained by an interaction of loop 3 by a set of hydrophobic contacts between subunits. Within these contacts, the side chain of a hydrophobic residue of one subunit fits into a cavity created by a set of hydrophobic residues in the neighboring subunit, via a "ball and socket" interaction. LvTIM presents a Cys47 at the "ball" inter-subunit contact indicating that the character of this residue is responsible for the decrease in dimer stability. Mutational studies show that this residue plays a role in dimer stability but is not a solely determinant for dimer formation. Structural insights from a novel invertebrate triosephosphate isomerase from Litopenaeus vannamei.,Lopez-Zavala AA, Carrasco-Miranda JS, Ramirez-Aguirre CD, Lopez-Hidalgo M, Benitez-Cardoza CG, Ochoa-Leyva A, Cardona-Felix CS, Diaz-Quezada C, Rudino-Pinera E, Sotelo-Mundo RR, Brieba LG Biochim Biophys Acta. 2016 Sep 7;1864(12):1696-1706. doi:, 10.1016/j.bbapap.2016.09.002. PMID:27614148[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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