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TitleCryo-EM structure of AMP-PNP-bound human mitochondrial ATP-binding cassette transporter ABCB7.
Journal, issue, pagesJ Struct Biol, Vol. 214, Issue 1, Page 107832, Year 2022
Publish dateJan 15, 2022
AuthorsQinqin Yan / Yuequan Shen / Xue Yang /
PubMed AbstractATP-binding cassette subfamily B member 7 (ABCB7) is localized in the inner membrane of mitochondria, playing a critical role in iron metabolism. Here, we determined the structure of the ...ATP-binding cassette subfamily B member 7 (ABCB7) is localized in the inner membrane of mitochondria, playing a critical role in iron metabolism. Here, we determined the structure of the nonhydrolyzable ATP analog adenosine-5'-(β-γ-imido) triphosphate (AMP-PNP) bound human ABCB7 at 3.3 Å by single-particle electron cryo-microscopy (cryo-EM). The AMP-PNP-bound human ABCB7 shows an inverted V-shaped homodimeric architecture with an inward-facing open conformation. One AMP-PNP molecule and Mg were identified in each nucleotide-binding domain (NBD) of the hABCB7 monomer. Moreover, four disease-causing missense mutations of human ABCB7 have been mapped to the structure, creating a hotspot map for X-linked sideroblastic anemia and ataxia disease. Our results provide a structural basis for further understanding the transport mechanism of the mitochondrial ABC transporter.
External linksJ Struct Biol / PubMed:35041979
MethodsEM (single particle)
Resolution3.3 Å
Structure data

31967

7vgf

EMDB-31967, PDB-7vgf:
cryo-EM structure of AMP-PNP bound human ABCB7
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / transporter / dimer / mitochondrial

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