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TitleCryo-EM structure of human ABCB8 transporter in nucleotide binding state.
Journal, issue, pagesBiochem Biophys Res Commun, Vol. 557, Page 187-191, Year 2021
Publish dateJun 11, 2021
AuthorsShunjin Li / Yue Ren / Xuhang Lu / Yuequan Shen / Xue Yang /
PubMed AbstractHuman ATP-binding cassette transporter 8 of subfamily B (hABCB8) is an ABC transporter that located in the inner membrane of mitochondria. The ABCB8 is involved in the maturation of Fe-S and protects ...Human ATP-binding cassette transporter 8 of subfamily B (hABCB8) is an ABC transporter that located in the inner membrane of mitochondria. The ABCB8 is involved in the maturation of Fe-S and protects the heart from oxidative stress. Here, we present the cryo-EM structure of human ABCB8 binding with AMPPNP in inward-facing conformation with resolution of 4.1 Å. hABCB8 shows an open-inward conformation when ATP is bound. Unexpectedly, cholesterol molecules were identified in the transmembrane domain of hABCB8. Our results provide structural basis for the transport mechanism of the ABC transporter in mitochondria.
External linksBiochem Biophys Res Commun / PubMed:33872987
MethodsEM (single particle)
Resolution4.1 Å
Structure data

31142

7ehl

EMDB-31142, PDB-7ehl:
Cryo-EM structure of human ABCB8 transporter in nucleotide binding state
Method: EM (single particle) / Resolution: 4.1 Å

Chemicals

ChemComp-CLR:
CHOLESTEROL

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

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / ABC transporter

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