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Structure paper

TitleMolecular basis of cholesterol efflux via ABCG subfamily transporters.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 118, Issue 34, Year 2021
Publish dateAug 24, 2021
AuthorsYingyuan Sun / Jin Wang / Tao Long / Xiaofeng Qi / Linda Donnelly / Nadia Elghobashi-Meinhardt / Leticia Esparza / Jonathan C Cohen / Xiao-Song Xie / Helen H Hobbs / Xiaochun Li /
PubMed AbstractThe ABCG1 homodimer (G1) and ABCG5-ABCG8 heterodimer (G5G8), two members of the adenosine triphosphate (ATP)-binding cassette (ABC) transporter G family, are required for maintenance of cellular ...The ABCG1 homodimer (G1) and ABCG5-ABCG8 heterodimer (G5G8), two members of the adenosine triphosphate (ATP)-binding cassette (ABC) transporter G family, are required for maintenance of cellular cholesterol levels. G5G8 mediates secretion of neutral sterols into bile and the gut lumen, whereas G1 transports cholesterol from macrophages to high-density lipoproteins (HDLs). The mechanisms used by G5G8 and G1 to recognize and export sterols remain unclear. Here, we report cryoelectron microscopy (cryo-EM) structures of human G5G8 in sterol-bound and human G1 in cholesterol- and ATP-bound states. Both transporters have a sterol-binding site that is accessible from the cytosolic leaflet. A second site is present midway through the transmembrane domains of G5G8. The Walker A motif of G8 adopts a unique conformation that accounts for the marked asymmetry in ATPase activities between the two nucleotide-binding sites of G5G8. These structures, along with functional validation studies, provide a mechanistic framework for understanding cholesterol efflux via ABC transporters.
External linksProc Natl Acad Sci U S A / PubMed:34404721 / PubMed Central
MethodsEM (single particle)
Resolution2.6 - 3.7 Å
Structure data

24310

7r87

EMDB-24310, PDB-7r87:
The structure of human ABCG5-WT/ABCG8-I419E
Method: EM (single particle) / Resolution: 3.4 Å

24311

7r88

EMDB-24311, PDB-7r88:
The structure of human ABCG5-I529W/ABCG8-WT
Method: EM (single particle) / Resolution: 3.5 Å

24312

7r89

EMDB-24312, PDB-7r89:
The structure of human ABCG5/ABCG8 purified from yeast
Method: EM (single particle) / Resolution: 2.6 Å

24313

7r8a

EMDB-24313, PDB-7r8a:
The structure of human ABCG5/ABCG8 purified from mammalian cells
Method: EM (single particle) / Resolution: 2.9 Å

24314

7r8b

EMDB-24314, PDB-7r8b:
The structure of human ABCG5/ABCG8 supplemented with cholesterol
Method: EM (single particle) / Resolution: 3.1 Å

24315

7r8c

EMDB-24315, PDB-7r8c:
The structure of human ABCG1
Method: EM (single particle) / Resolution: 3.7 Å

24316

7r8d

EMDB-24316, PDB-7r8d:
The structure of human ABCG1 E242Q with cholesterol
Method: EM (single particle) / Resolution: 3.2 Å

24317

7r8e

EMDB-24317, PDB-7r8e:
The structure of human ABCG1 E242Q complexed with ATP
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

ChemComp-ERG:
ERGOSTEROL / Ergosterol

ChemComp-CLR:
CHOLESTEROL / Cholesterol

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

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsLIPID TRANSPORT/IMMUNE SYSTEM / sterol / lipids / ABC transporter / LIPID TRANSPORT / LIPID TRANSPORT-IMMUNE SYSTEM complex

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