Structural basis of substrate recognition and translocation by human very long-chain fatty acid transporter ABCD1
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Abstract
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.
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ALDP transport involves cooperative binding of two VLCFAcyl-CoAs, ATP binding, and ALDP homodimerization, followed by outward-facing conformational change allowing release of VLCFAcylCoA into the peroxisome matrix, where VLCFAcyl-CoA undergoes peroxisomal β-oxidation.
“Transport involves cooperative binding of two VLCFAcyl-CoAs, ATP binding, and ALDP homodimerization [147], followed by outward-facing ALDP conformational change allowing for the release of VLCFAcylCoA into the peroxisome matrix [148], where VLCFAcyl-CoA undergoes peroxisomal β-oxidation [149].”
From Revisiting the Pathogenesis of X-Linked Adrenoleukodystrophy (2025) · cites this paper as [148]
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Metabolic modeling with reverse mapping links host perturbations to Mycobacterium tuberculosis
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- Authors
- Chen, Z.-P., Xu, D., Wang, L., Mao, Y.-X., Li, Y., Cheng, M.-T., Zhou, C.-Z., Hou, W.-T., & Chen, Y.
- Affiliations
- University of Science and Technology of China (CN)
- Corresponding author
- Zhou, Cong-Zhao
- Hou, Wen-Tao
- Chen, Yuxing
- Venue
- Nature Communications
- Published
- 2022-06-08
- Volume
- 13
- Issue
- 1
- Pages
- 3299-3299
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC9177597
- OpenAlex
- W4281625653
- Cited by
- 37
- References
- 76
- Citations by year
- 2026: 6 · 2025: 9 · 2024: 8 · 2023: 7 · 2022: 6 · 2021: 1
- FWCI
- 3.14
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Ministry of Science and Technology of the People's Republic of China (2020YFA0509302)
- National Natural Science Foundation of China (32071206)
- The Strategic Priority Research Program of the Chinese Academy of Sciences
- Topics
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- ABCD1, ABC transporters, X-linked adrenoleukodystrophy, peroxisomal beta-oxidation, substrate recognition, substrate translocation, ATP-bound state, transmembrane domain, cryo-EM structure, pantothenic acid
- MeSH terms
- ATP Binding Cassette Transporter, Subfamily D, Member 1, Adrenoleukodystrophy, Coenzyme A, Fatty Acids, Nonesterified, Humans, Peroxisomes
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