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TitleCryo-EM structures of human ABCA7 provide insights into its phospholipid translocation mechanisms.
Journal, issue, pagesEMBO J, Vol. 42, Issue 3, Page e111065, Year 2023
Publish dateFeb 1, 2023
AuthorsLe Thi My Le / James Robert Thompson / Sepehr Dehghani-Ghahnaviyeh / Shashank Pant / Phuoc Xuan Dang / Jarrod Bradley French / Takahisa Kanikeyo / Emad Tajkhorshid / Amer Alam /
PubMed AbstractPhospholipid extrusion by ABC subfamily A (ABCA) exporters is central to cellular physiology, although the specifics of the underlying substrate interactions and transport mechanisms remain poorly ...Phospholipid extrusion by ABC subfamily A (ABCA) exporters is central to cellular physiology, although the specifics of the underlying substrate interactions and transport mechanisms remain poorly resolved at the molecular level. Here we report cryo-EM structures of lipid-embedded human ABCA7 in an open state and in a nucleotide-bound, closed state at resolutions between 3.6 and 4.0 Å. The former reveals an ordered patch of bilayer lipids traversing the transmembrane domain (TMD), while the latter reveals a lipid-free, closed TMD with a small extracellular opening. These structures offer a structural framework for both substrate entry and exit from the ABCA7 TMD and highlight conserved rigid-body motions that underlie the associated conformational transitions. Combined with functional analysis and molecular dynamics (MD) simulations, our data also shed light on lipid partitioning into the ABCA7 TMD and localized membrane perturbations that underlie ABCA7 function and have broader implications for other ABCA family transporters.
External linksEMBO J / PubMed:36484366 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 4.0 Å
Structure data

28041

8edw

EMDB-28041, PDB-8edw:
Cryo-EM Structure of human ABCA7 in BPL/Ch Nanodiscs
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-28044: Human ABCA7 in BPL/Ch nanodiscs (Map 2)
Method: EM (single particle) / Resolution: 3.2 Å

28047

8ee6

EMDB-28047, PDB-8ee6:
Cryo-EM Structure of human ABCA7 in PE/Ch nanodiscs
Method: EM (single particle) / Resolution: 4.0 Å

28050

8eeb

EMDB-28050, PDB-8eeb:
Cryo-EM structure of human ABCA7 in Digitonin
Method: EM (single particle) / Resolution: 3.9 Å

28451

8eop

EMDB-28451, PDB-8eop:
Cryo-EM Structure of Nanodisc reconstituted human ABCA7 EQ mutant in ATP bound closed state
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose


ChemComp, No image

ChemComp-UNL:
Unknown ligand

ChemComp-AGS:
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogue*YM

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

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / ABC transporter / Lipid Transporter / ABC exporter

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