6nxw: Difference between revisions

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 <StructureSection load='6nxw' size='340' side='right'caption='[[6nxw]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6nxw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NXW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6NXW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6nxw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NXW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NXW FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTIMC, At3g55440, T22E16.100 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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]] 1.95&#8491;</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=6nxw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nxw OCA], [https://pdbe.org/6nxw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nxw RCSB], [https://www.ebi.ac.uk/pdbsum/6nxw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nxw ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6nxw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nxw OCA], [http://pdbe.org/6nxw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nxw RCSB], [http://www.ebi.ac.uk/pdbsum/6nxw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nxw ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/TPIS_ARATH TPIS_ARATH]
-Reactive oxidative species (ROS) and S-glutathionylation modulate the activity of plant cytosolic triosephosphate isomerases (cTPI). Arabidopsis thaliana cTPI (AtcTPI) is subject of redox regulation at two reactive cysteines that function as thiol switches. Here we investigate the role of these residues, AtcTPI-Cys13 and At-Cys218, by substituting them with aspartic acid that mimics the irreversible oxidation of cysteine to sulfinic acid and with amino acids that mimic thiol conjugation. Crystallographic studies show that mimicking AtcTPI-Cys13 oxidation promotes the formation of inactive monomers by reposition residue Phe75 of the neighboring subunit, into a conformation that destabilizes the dimer interface. Mutations in residue AtcTPI-Cys218 to Asp, Lys, or Tyr generate TPI variants with a decreased enzymatic activity by creating structural modifications in two loops (loop 7 and loop 6) whose integrity is necessary to assemble the active site. In contrast with mutations in residue AtcTPI-Cys13, mutations in AtcTPI-Cys218 do not alter the dimeric nature of AtcTPI. Therefore, modifications of residues AtcTPI-Cys13 and AtcTPI-Cys218 modulate AtcTPI activity by inducing the formation of inactive monomers and by altering the active site of the dimeric enzyme, respectively. The identity of residue AtcTPI-Cys218 is conserved in the majority of plant cytosolic TPIs, this conservation and its solvent-exposed localization make it the most probable target for TPI regulation upon oxidative damage by reactive oxygen species. Our data reveal the structural mechanisms by which S-glutathionylation protects AtcTPI from irreversible chemical modifications and re-routes carbon metabolism to the pentose phosphate pathway to decrease oxidative stress.
-Structural basis for the modulation of plant cytosolic triosephosphate isomerase activity by mimicry of redox-based modifications.,Castro-Torres E, Jimenez-Sandoval P, Romero-Romero S, Fuentes-Pascacio A, Lopez-Castillo LM, Diaz-Quezada C, Fernandez-Velasco DA, Torres-Larios A, Brieba LG Plant J. 2019 Sep;99(5):950-964. doi: 10.1111/tpj.14375. Epub 2019 Jun 13. PMID:31034710<ref>PMID:31034710</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 6nxw" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Arath]]
+[[Category: Arabidopsis thaliana]]
 [[Category: Large Structures]]
-[[Category: Triose-phosphate isomerase]]
+[[Category: Brieba LG]]
-[[Category: Brieba, L G]]
+[[Category: Diaz-Quezada C]]
-[[Category: Diaz-Quezada, C]]
+[[Category: Jimenez-Sandoval P]]
-[[Category: Jimenez-Sandoval, P]]
+[[Category: Torres-Larios A]]
-[[Category: Torres-Larios, A]]
-[[Category: Isomerase]]
-[[Category: Triosephosphate isomerase crystal structure mutant dimer redox regulation]]