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==Cryo-EM structure of C22:0-CoA bound human very long-chain fatty acid ABC transporter ABCD1==
<StructureSection load='7vzb' size='340' side='right'caption='[[7vzb]], [[Resolution|resolution]] 3.59&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7vzb]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VZB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VZB FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FFI:S-[2-[3-[[(2R)-4-[[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethyl]+docosanethioate'>FFI</scene>, <scene name='pdbligand=Y01:CHOLESTEROL+HEMISUCCINATE'>Y01</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=7vzb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vzb OCA], [https://pdbe.org/7vzb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vzb RCSB], [https://www.ebi.ac.uk/pdbsum/7vzb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vzb ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human ABC transporter ABCD1 transports very long-chain fatty acids from cytosol to peroxisome for beta-oxidation, dysfunction of which usually causes the X-linked adrenoleukodystrophy (X-ALD). Here, we report three cryogenic electron microscopy structures of ABCD1: the apo-form, substrate- and ATP-bound forms. Distinct from what was seen in the previously reported ABC transporters, the two symmetric molecules of behenoyl coenzyme A (C22:0-CoA) cooperatively bind to the transmembrane domains (TMDs). For each C22:0-CoA, the hydrophilic 3'-phospho-ADP moiety of CoA portion inserts into one TMD, with the succeeding pantothenate and cysteamine moiety crossing the inter-domain cavity, whereas the hydrophobic fatty acyl chain extends to the opposite TMD. Structural analysis combined with biochemical assays illustrates snapshots of ABCD1-mediated substrate transport cycle. It advances our understanding on the selective oxidation of fatty acids and molecular pathology of X-ALD.

Structural basis of substrate recognition and translocation by human very long-chain fatty acid transporter ABCD1.,Chen ZP, Xu D, Wang L, Mao YX, Li Y, Cheng MT, Zhou CZ, Hou WT, Chen Y Nat Commun. 2022 Jun 8;13(1):3299. doi: 10.1038/s41467-022-30974-5. PMID:35676282<ref>PMID:35676282</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7vzb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Chen, Y X]]
[[Category: Chen, Z P]]
[[Category: Cheng, M T]]
[[Category: Hou, W T]]
[[Category: Mao, Y X]]
[[Category: Wang, L]]
[[Category: Xu, D]]
[[Category: Yang, L]]
[[Category: Zhou, C Z]]
[[Category: Abc transporter]]
[[Category: Peroxisome]]
[[Category: Transport protein]]
[[Category: Very long-chain fatty]]