Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2022 Feb;32(2):214-217.
doi: 10.1038/s41422-021-00585-8. Epub 2021 Nov 9.

Structural basis of acyl-CoA transport across the peroxisomal membrane by human ABCD1

Rong Wang  1 , Yu Qin  1 , Xiaochun Li  2   3
Affiliations

Structural basis of acyl-CoA transport across the peroxisomal membrane by human ABCD1

Rong Wang et al. Cell Res. 2022 Feb.
No abstract available

PubMed Disclaimer

Conflict of interest statement

The authors declare no competing interests.

Figures

Fig. 1
Fig. 1. Cryo-EM structures of human ABCD1EQ in oleoyl-CoA-bound and ATP-bound conformations.
a Overall structures of human ABCD1EQ in oleoyl-CoA- and ATP-bound conformations. Oleoyl-CoA and ATP are shown with magenta and yellow sticks. b Topology diagram for ABCD1 protomer. Secondary and key structural elements of TMD are indicated. c Interaction details of oleoyl-CoA and ABCD1EQ. Cryo-EM map of oleoyl-CoA are shown at 3.5 σ level. Hydrogen bonds are labeled by dash lines, and residues that were validated by the binding assay are underlined. d The fNBD-oleoyl-CoA binding assay between WT or ABCD1 variants and fNBD-oleoyl-CoA. ****P < 0.0001, **P < 0.001. Data are means ± SD (n = 3). e Superposition of human ABCD1EQ and human ABCD4EQ (PDB: 6JBJ). ABCD1EQ is indicated same as (a), while ABCD4EQ is colored in gray. f Structural comparison of the ATP binding sites in ABCD1EQ and ABCD4EQ. Walker A of ABCD1EQ is shown in wheat. Specific residues in the signature motif are highlighted in red. g Structural comparison of oleoyl-CoA-bound ABCD1EQ and ATP-bound ABCD1EQ protomers. Structural movements after ATP binding are indicated by black arrows. h ABCD1 employs a distinct recognition mechanism in comparison with ABCB4 (PDB: 7NIV) and MsbA (PDB: 5TV4). i A proposed model for acyl-CoA or fatty acids recruitment and transport by human ABCD1 in peroxisome. First, ABCD1 in the cytosol-facing conformation is ready to bind substrates, then two molecules of acyl-CoA or fatty acids can be recognized by one ABCD1 homodimer. ABCD1 will further undergo a dramatic conformational change when ATP is engaged by NBDs, leading to the release of these substrates to the peroxisome lumen. After ATP hydrolysis, ABCD1 returns to the resting state.
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Kawaguchi K, Morita M. Biomed. Res. Int. 2016;2016:6786245. doi: 10.1155/2016/6786245. - DOI - PMC - PubMed
    1. Hlavac V, Soucek P. Biochem. Soc. Trans. 2015;43:937–942. doi: 10.1042/BST20150114. - DOI - PubMed
    1. Xu D, et al. Cell Res. 2019;29:1039–1041. doi: 10.1038/s41422-019-0222-z. - DOI - PMC - PubMed
    1. Jia, Y. et al. bioRxiv, 10.1101/2021.09.24.461756 (2021).
    1. My Le, L. T. et al. bioRxiv, 10.1101/2021.09.04.458904 (2021).

Publication types

Substances