6yaw
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==Crystal structure of human GSTA1-1 bound to the glutathione adduct of cinnamaldehyde== | ==Crystal structure of human GSTA1-1 bound to the glutathione adduct of cinnamaldehyde== | ||
| - | <StructureSection load='6yaw' size='340' side='right'caption='[[6yaw]]' scene=''> | + | <StructureSection load='6yaw' size='340' side='right'caption='[[6yaw]], [[Resolution|resolution]] 2.19Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YAW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6YAW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6yaw]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YAW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6YAW FirstGlance]. <br> |
| - | </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=6yaw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yaw OCA], [http://pdbe.org/6yaw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6yaw RCSB], [http://www.ebi.ac.uk/pdbsum/6yaw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6yaw ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=P9H:(2~{S})-2-azanyl-5-[[(2~{R})-1-(2-hydroxy-2-oxoethylamino)-1-oxidanylidene-3-[(1~{R})-3-oxidanylidene-1-phenyl-propyl]sulfanyl-propan-2-yl]amino]-5-oxidanylidene-pentanoic+acid'>P9H</scene></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=6yaw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yaw OCA], [http://pdbe.org/6yaw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6yaw RCSB], [http://www.ebi.ac.uk/pdbsum/6yaw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6yaw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/GSTA1_HUMAN GSTA1_HUMAN]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.<ref>PMID:20606271</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Xenobiotic metabolizing enzymes and other proteins, including odorant-binding proteins located in the nasal epithelium and mucus, participate in a series of processes modulating the concentration of odorants in the environment of olfactory receptors and finely impact odor perception. These enzymes and transporters are thought to participate in odorant degradation or transport. Odorant biotransformation results in (i) changes in the odorant quantity up to their clearance and the termination of signalling and (ii) the formation of new odorant stimuli (metabolites). Enzymes, such as cytochrome P450 and glutathione transferases (GSTs), have been proposed to participate in odorant clearance in insects and mammals as odorant metabolizing enzymes. This study aims to explore the function of GSTs in human olfaction. Using immunohistochemical methods, GSTs were found to be localized in human tissues surrounding the olfactory epithelium. Then, the activity of two members of the GST family towards odorants was measured using heterologously expressed enzymes. The interactions/reactions with odorants were further characterized using a combination of enzymatic techniques. Furthermore, the structure of the complex between human GSTA1 and the glutathione conjugate of an odorant was determined by X-ray crystallography. Our results strongly suggest the role of human GSTs in the modulation of odorant availability to olfactory receptors in the peripheral olfactory process. | ||
| + | |||
| + | Interactions between Odorants and Glutathione Transferases in the Human Olfactory Cleft.,Schwartz M, Menetrier F, Heydel JM, Chavanne E, Faure P, Labrousse M, Lirussi F, Canon F, Mannervik B, Briand L, Neiers F Chem Senses. 2020 Aug 21. pii: 5895478. doi: 10.1093/chemse/bjaa055. PMID:32822468<ref>PMID:32822468</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6yaw" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Neiers F]] | + | [[Category: Neiers, F]] |
| - | [[Category: Schwartz M]] | + | [[Category: Schwartz, M]] |
| + | [[Category: Detoxification]] | ||
| + | [[Category: Glutathione transferase]] | ||
| + | [[Category: Metabolism]] | ||
| + | [[Category: Olfaction]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 07:11, 2 September 2020
Crystal structure of human GSTA1-1 bound to the glutathione adduct of cinnamaldehyde
| |||||||||||
