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Structure paper

TitleStructural basis of substrate recognition and translocation by human very long-chain fatty acid transporter ABCD1.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 3299, Year 2022
Publish dateJun 8, 2022
AuthorsZhi-Peng Chen / Da Xu / Liang Wang / Yao-Xu Mao / Yang Li / Meng-Ting Cheng / Cong-Zhao Zhou / Wen-Tao Hou / Yuxing Chen /
PubMed AbstractHuman ABC transporter ABCD1 transports very long-chain fatty acids from cytosol to peroxisome for β-oxidation, dysfunction of which usually causes the X-linked adrenoleukodystrophy (X-ALD). Here, we ...Human ABC transporter ABCD1 transports very long-chain fatty acids from cytosol to peroxisome for β-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.
External linksNat Commun / PubMed:35676282 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 3.59 Å
Structure data

32152

7vwc

EMDB-32152, PDB-7vwc:
Cryo-EM structure of human very long-chain fatty acid ABC transporter ABCD1
Method: EM (single particle) / Resolution: 3.53 Å

32171

7vx8

EMDB-32171, PDB-7vx8:
Cryo-EM structure of ATP-bound human very long-chain fatty acid ABC transporter ABCD1
Method: EM (single particle) / Resolution: 2.8 Å

32224

7vzb

EMDB-32224, PDB-7vzb:
Cryo-EM structure of C22:0-CoA bound human very long-chain fatty acid ABC transporter ABCD1
Method: EM (single particle) / Resolution: 3.59 Å

Chemicals

ChemComp-82T:
[(2R)-3-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-2-oxidanyl-propyl] octadecanoate

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

ChemComp-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

Source
  • caenorhabditis elegans (invertebrata)
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / very long-chain fatty / Peroxisome / ABC transporter

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