7aia: Difference between revisions
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New page: '''Unreleased structure''' The entry 7aia is ON HOLD Authors: Nguyen, G.T.T., Sutinen, A., Kursula, P. Description: Complex of human GDAP1 with hexadecanedioic acid [[Category: Unrelea... |
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The | ==Complex of human GDAP1 with hexadecanedioic acid== | ||
<StructureSection load='7aia' size='340' side='right'caption='[[7aia]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AIA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AIA 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]] 2.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=RF8:hexadecanedioic+acid'>RF8</scene></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=7aia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7aia OCA], [https://pdbe.org/7aia PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7aia RCSB], [https://www.ebi.ac.uk/pdbsum/7aia PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7aia ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Charcot-Marie-Tooth disease (CMT) is one of the most common inherited neurological disorders. Despite the common involvement of ganglioside-induced differentiation-associated protein 1 (GDAP1) in CMT, the protein structure and function, as well as the pathogenic mechanisms, remain unclear. We determined the crystal structure of the complete human GDAP1 core domain, which shows a novel mode of dimerization within the glutathione S-transferase (GST) family. The long GDAP1-specific insertion forms an extended helix and a flexible loop. GDAP1 is catalytically inactive toward classical GST substrates. Through metabolite screening, we identified a ligand for GDAP1, the fatty acid hexadecanedioic acid, which is relevant for mitochondrial membrane permeability and Ca(2+) homeostasis. The fatty acid binds to a pocket next to a CMT-linked residue cluster, increases protein stability, and induces changes in protein conformation and oligomerization. The closest homologue of GDAP1, GDAP1L1, is monomeric in its full-length form. Our results highlight the uniqueness of GDAP1 within the GST family and point toward allosteric mechanisms in regulating GDAP1 oligomeric state and function. | |||
Structure of the Complete Dimeric Human GDAP1 Core Domain Provides Insights into Ligand Binding and Clustering of Disease Mutations.,Nguyen GTT, Sutinen A, Raasakka A, Muruganandam G, Loris R, Kursula P Front Mol Biosci. 2021 Jan 27;7:631232. doi: 10.3389/fmolb.2020.631232. , eCollection 2020. PMID:33585569<ref>PMID:33585569</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Kursula | <div class="pdbe-citations 7aia" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Kursula P]] | |||
[[Category: Nguyen GTT]] | |||
[[Category: Sutinen A]] | |||
Latest revision as of 06:03, 21 November 2024
Complex of human GDAP1 with hexadecanedioic acid
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