7alm: Difference between revisions

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'''Unreleased structure'''


The entry 7alm is ON HOLD
==Crystal structure of human GDAP1 at 2.8 Angstrom resolution.==
<StructureSection load='7alm' size='340' side='right'caption='[[7alm]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ALM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ALM 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]] 2.8&#8491;</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=7alm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7alm OCA], [https://pdbe.org/7alm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7alm RCSB], [https://www.ebi.ac.uk/pdbsum/7alm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7alm 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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 7alm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Kursula P]]
[[Category: Nguyen GTT]]
[[Category: Raasakka A]]
[[Category: Sutinen A]]
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