9f7k

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'''Unreleased structure'''
 
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The entry 9f7k is ON HOLD
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==Glutathione transferase epsilon 1 from Drosophila melanogaster in complex with glutathione==
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<StructureSection load='9f7k' size='340' side='right'caption='[[9f7k]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9f7k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster_American_nodavirus_(ANV)_SW-2009a Drosophila melanogaster American nodavirus (ANV) SW-2009a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9F7K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9F7K FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9f7k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9f7k OCA], [https://pdbe.org/9f7k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9f7k RCSB], [https://www.ebi.ac.uk/pdbsum/9f7k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9f7k ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q7KK90_DROME Q7KK90_DROME]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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This study presents a comprehensive analysis of the dimerization interfaces of fly GSTs through sequence alignment. Our investigation revealed GSTE1 as a particularly intriguing target, providing valuable insights into the variations within Delta and Epsilon GST interfaces. The X-ray structure of GSTE1 was determined, unveiling remarkable thermal stability and a distinctive dimerization interface. Utilizing circular dichroism, we assessed the thermal stability of GSTE1 and other Drosophila GSTs with resolved X-ray structures. The subsequent examination of GST dimer stability correlated with the dimerization interface supported by findings from X-ray structural analysis and thermal stability measurements. Our discussion extends to the broader context of GST dimer interfaces, offering a generalized perspective on their stability. This research enhances our understanding of the structural and thermodynamic aspects of GST dimerization, contributing valuable insights to the field.
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Authors: Didierjean, C., Schwartz, M., Neiers, F.
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Structural and Thermodynamic Insights into Dimerization Interfaces of Drosophila Glutathione Transferases.,Schwartz M, Petiot N, Chaloyard J, Senty-Segault V, Lirussi F, Senet P, Nicolai A, Heydel JM, Canon F, Sonkaria S, Khare V, Didierjean C, Neiers F Biomolecules. 2024 Jun 26;14(7):758. doi: 10.3390/biom14070758. PMID:39062472<ref>PMID:39062472</ref>
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Description: Glutathione transferase epsilon 1 from Drosophila melanogaster in complex with glutathione
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Schwartz, M]]
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<div class="pdbe-citations 9f7k" style="background-color:#fffaf0;"></div>
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[[Category: Didierjean, C]]
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== References ==
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[[Category: Neiers, F]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Didierjean C]]
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[[Category: Neiers F]]
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[[Category: Schwartz M]]

Current revision

Glutathione transferase epsilon 1 from Drosophila melanogaster in complex with glutathione

PDB ID 9f7k

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