7vwc

Cryo-EM structure of human very long-chain fatty acid ABC transporter ABCD1

spinqualitylabelsall models 7vwc, resolution 3.53Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7vwc is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 82T Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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