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TitleCryo-EM structures of the human surfactant lipid transporter ABCA3.
Journal, issue, pagesSci Adv, Vol. 8, Issue 14, Page eabn3727, Year 2022
Publish dateApr 8, 2022
AuthorsTian Xie / Zike Zhang / Jian Yue / Qi Fang / Xin Gong /
PubMed AbstractThe adenosine 5'-triphosphate (ATP)-binding cassette (ABC) transporter ABCA3 plays a critical role in pulmonary surfactant biogenesis. Mutations in human ABCA3 have been recognized as the most ...The adenosine 5'-triphosphate (ATP)-binding cassette (ABC) transporter ABCA3 plays a critical role in pulmonary surfactant biogenesis. Mutations in human ABCA3 have been recognized as the most frequent causes of inherited surfactant dysfunction disorders. Despite two decades of research, in vitro biochemical and structural studies of ABCA3 are still lacking. Here, we report the cryo-EM structures of human ABCA3 in two distinct conformations, both at resolution of 3.3 Å. In the absence of ATP, ABCA3 adopts a "lateral-opening" conformation with the lateral surfaces of transmembrane domains (TMDs) exposed to the membrane and features two positively charged cavities within the TMDs as potential substrate binding sites. ATP binding induces pronounced conformational changes, resulting in the collapse of the potential substrate binding cavities. Our results help to rationalize the disease-causing mutations in human ABCA3 and suggest a conserved "lateral access and extrusion" mechanism for both lipid export and import mediated by ABCA transporters.
External linksSci Adv / PubMed:35394827 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 6.3 Å
Structure data

32233

7w01

EMDB-32233, PDB-7w01:
Cryo-EM structure of nucleotide-free ABCA3
Method: EM (single particle) / Resolution: 3.3 Å

32234

7w02

EMDB-32234, PDB-7w02:
Cryo-EM structure of ATP-bound ABCA3
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-32235: Cryo-EM map of nucleotide-free ABCA3 in LMNG/CHS
Method: EM (single particle) / Resolution: 6.3 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-PX4:
1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / DMPC, phospholipid*YM / Dimyristoylphosphatidylcholine

ChemComp-POV:
(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate / phospholipid*YM / POPC

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsTRANSLOCASE / ABC transporter / MEMBRANE PROTEIN

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