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TitleCryo-EM structures of mitochondrial ABC transporter ABCB10 in apo and biliverdin-bound form.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 2030, Year 2023
Publish dateApr 11, 2023
AuthorsSheng Cao / Yihu Yang / Lili He / Yumo Hang / Xiaodong Yan / Hui Shi / Jiaquan Wu / Zhuqing Ouyang /
PubMed AbstractABCB10, 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 ...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.
External linksNat Commun / PubMed:37041204 / PubMed Central
MethodsEM (single particle)
Resolution2.85 - 3.67 Å
Structure data

EMDB-33603, PDB-7y48:
Cryo-EM Structure of biliverdin-bound mitochondrial ABC transporter ABCB10 from Biortus
Method: EM (single particle) / Resolution: 2.85 Å

EMDB-33604, PDB-7y49:
Cryo-EM Structure of apo mitochondrial ABC transporter ABCB10 from Biortus
Method: EM (single particle) / Resolution: 3.67 Å

Chemicals

ChemComp-CLR:
CHOLESTEROL

ChemComp-IE5:
Biliverdine IX Alpha

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / ABC transporter / biliverdin / ABCB10

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