Structures of Atm1 provide insight into [2Fe-2S] cluster export from mitochondria

Ping Li, Amber L. Hendricks, Yong Wang, Rhiza Lyne E. Villones, Karin Lindkvist-Petersson, Gabriele Meloni, J. A. Cowan, Kaituo Wang () and Pontus Gourdon ()
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Ping Li: Lund University
Amber L. Hendricks: The Ohio State University
Yong Wang: Zhejiang University
Rhiza Lyne E. Villones: The University of Texas at Dallas
Karin Lindkvist-Petersson: Lund University
Gabriele Meloni: The University of Texas at Dallas
J. A. Cowan: The Ohio State University
Kaituo Wang: Copenhagen University
Pontus Gourdon: Lund University

Nature Communications, 2022, vol. 13, issue 1, 1-12

Abstract: Abstract In eukaryotes, iron-sulfur clusters are essential cofactors for numerous physiological processes, but these clusters are primarily biosynthesized in mitochondria. Previous studies suggest mitochondrial ABCB7-type exporters are involved in maturation of cytosolic iron-sulfur proteins. However, the molecular mechanism for how the ABCB7-type exporters participate in this process remains elusive. Here, we report a series of cryo-electron microscopy structures of a eukaryotic homolog of human ABCB7, CtAtm1, determined at average resolutions ranging from 2.8 to 3.2 Å, complemented by functional characterization and molecular docking in silico. We propose that CtAtm1 accepts delivery from glutathione-complexed iron-sulfur clusters. A partially occluded state links cargo-binding to residues at the mitochondrial matrix interface that line a positively charged cavity, while the binding region becomes internalized and is partially divided in an early occluded state. Collectively, our findings substantially increase the understanding of the transport mechanism of eukaryotic ABCB7-type proteins.

Date: 2022
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DOI: 10.1038/s41467-022-32006-8

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