Structural basis of substrate recognition and translocation by human very long-chain fatty acid transporter ABCD1

Zhi-Peng Chen; Da Xu; Liang Wang; Yao-Xu Mao; Yang Li; Meng-Ting Cheng; Cong-Zhao Zhou; Wen-Tao Hou; Yuxing Chen

doi:10.1038/s41467-022-30974-5

Nature Communications (Jun 2022)

Structural basis of substrate recognition and translocation by human very long-chain fatty acid transporter ABCD1

Zhi-Peng Chen,
Da Xu,
Liang Wang,
Yao-Xu Mao,
Yang Li,
Meng-Ting Cheng,
Cong-Zhao Zhou,
Wen-Tao Hou,
Yuxing Chen

Affiliations

Zhi-Peng Chen: School of Life Sciences, University of Science and Technology of China
Da Xu: School of Life Sciences, University of Science and Technology of China
Liang Wang: School of Life Sciences, University of Science and Technology of China
Yao-Xu Mao: School of Life Sciences, University of Science and Technology of China
Yang Li: School of Life Sciences, University of Science and Technology of China
Meng-Ting Cheng: School of Life Sciences, University of Science and Technology of China
Cong-Zhao Zhou: School of Life Sciences, University of Science and Technology of China
Wen-Tao Hou: School of Life Sciences, University of Science and Technology of China
Yuxing Chen: School of Life Sciences, University of Science and Technology of China

DOI: https://doi.org/10.1038/s41467-022-30974-5
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 10

Abstract

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Human ABC transporter ABCD1 transports very long-chain fatty acids from cytosol to peroxisome for βoxidation, dysfunction of which causes the X-ALD. Here, the authors report three structures of ABCD1: the ligand-free, C22:0-CoA- and ATP-bound forms.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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