Cryo-EM structures of mitochondrial ABC transporter ABCB10 in apo and biliverdin-bound form.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
11 04 2023
11 04 2023
Historique:
received:
14
07
2022
accepted:
03
04
2023
medline:
13
4
2023
entrez:
11
4
2023
pubmed:
12
4
2023
Statut:
epublish
Résumé
ABCB10, a member of ABC transporter superfamily that locates in the inner membrane of mitochondria, plays crucial roles in hemoglobin synthesis, antioxidative stress and stabilization of the iron transporter mitoferrin-1. Recently, it was found that ABCB10 is a mitochondrial biliverdin exporter. However, the molecular mechanism of biliverdin export by ABCB10 remains elusive. Here we report the cryo-EM structures of ABCB10 in apo (ABCB10-apo) and biliverdin-bound form (ABCB10-BV) at 3.67 Å and 2.85 Å resolution, respectively. ABCB10-apo adopts a wide-open conformation and may thus represent the apo form structure. ABCB10-BV forms a closed conformation and biliverdin situates in a hydrophobic pocket in one protomer and bridges the interaction through hydrogen bonds with the opposing one. We also identify cholesterols sandwiched by BVs and discuss the export dynamics based on these structural and biochemical observations.
Identifiants
pubmed: 37041204
doi: 10.1038/s41467-023-37851-9
pii: 10.1038/s41467-023-37851-9
pmc: PMC10090120
doi:
Substances chimiques
ATP-Binding Cassette Transporters
0
Biliverdine
O9MIA842K9
Membrane Transport Proteins
0
Mitochondrial Membrane Transport Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2030Informations de copyright
© 2023. The Author(s).
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