8q89
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 8q89 is ON HOLD until 2024-09-15 Authors: Schwartz, M., Neiers, F. Description: Crystal structure of Apis mellifera glutathione transferase delta 1...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Apis mellifera glutathione transferase delta 1 in a covalent dimeric state== | |
| + | <StructureSection load='8q89' size='340' side='right'caption='[[8q89]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8q89]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8Q89 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8Q89 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05Å</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=8q89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8q89 OCA], [https://pdbe.org/8q89 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8q89 RCSB], [https://www.ebi.ac.uk/pdbsum/8q89 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8q89 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A7M7GUY7_APIME A0A7M7GUY7_APIME] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Glutathione transferases (GST) are detoxification enzymes that conjugate glutathione to a wide array of molecules. In the honey bee Apis mellifera, AmGSTD1 is the sole member of the delta class of GSTs, with expression in antennae. Here, we structurally and biochemically characterized AmGSTD1 to elucidate its function. We showed that AmGSTD1 can efficiently catalyse the glutathione conjugation of classical GST substrates. Additionally, AmGSTD1 exhibits binding properties with a range of odorant compounds. AmGSTD1 has a peculiar interface with a structural motif we propose to call 'sulfur sandwich'. This motif consists of a cysteine disulfide bridge sandwiched between the sulfur atoms of two methionine residues and is stabilized by CH...S hydrogen bonds and S...S sigma-hole interactions. Thermal stability studies confirmed that this motif is important for AmGSTD1 stability and, thus, could facilitate its functions in olfaction. | ||
| - | + | Structure-activity analysis suggests an olfactory function for the unique antennal delta glutathione transferase of Apis mellifera.,Schwartz M, Boichot V, Muradova M, Fournier P, Senet P, Nicolai A, Canon F, Lirussi F, Ladeira R, Maibeche M, Chertemps T, Aubert E, Didierjean C, Neiers F FEBS Lett. 2023 Dec;597(24):3038-3048. doi: 10.1002/1873-3468.14770. Epub 2023 , Nov 7. PMID:37933500<ref>PMID:37933500</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Neiers | + | <div class="pdbe-citations 8q89" style="background-color:#fffaf0;"></div> |
| - | [[Category: Schwartz | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Apis mellifera]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Neiers F]] | ||
| + | [[Category: Schwartz M]] | ||
Current revision
Crystal structure of Apis mellifera glutathione transferase delta 1 in a covalent dimeric state
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