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TitleStructural basis of substrate recognition and translocation by human ABCA4.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 3853, Year 2021
Publish dateJun 22, 2021
AuthorsTian Xie / Zike Zhang / Qi Fang / Bowen Du / Xin Gong /
PubMed AbstractHuman ATP-binding cassette (ABC) subfamily A (ABCA) transporters mediate the transport of various lipid compounds across the membrane. Mutations in human ABCA transporters have been described to ...Human ATP-binding cassette (ABC) subfamily A (ABCA) transporters mediate the transport of various lipid compounds across the membrane. Mutations in human ABCA transporters have been described to cause severe hereditary disorders associated with impaired lipid transport. However, little is known about the mechanistic details of substrate recognition and translocation by ABCA transporters. Here, we present three cryo-EM structures of human ABCA4, a retina-specific ABCA transporter, in distinct functional states at resolutions of 3.3-3.4 Å. In the nucleotide-free state, the two transmembrane domains (TMDs) exhibit a lateral-opening conformation, allowing the lateral entry of substrate from the lipid bilayer. The N-retinylidene-phosphatidylethanolamine (NRPE), the physiological lipid substrate of ABCA4, is sandwiched between the two TMDs in the luminal leaflet and is further stabilized by an extended loop from extracellular domain 1. In the ATP-bound state, the two TMDs display a closed conformation, which precludes the substrate binding. Our study provides a molecular basis to understand the mechanism of ABCA4-mediated NRPE recognition and translocation, and suggests a common 'lateral access and extrusion' mechanism for ABCA-mediated lipid transport.
External linksNat Commun / PubMed:34158497 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 3.4 Å
Structure data

31000

7e7i

EMDB-31000, PDB-7e7i:
Cryo-EM structure of human ABCA4 in the apo state
Method: EM (single particle) / Resolution: 3.3 Å

31001

7e7o

EMDB-31001, PDB-7e7o:
Cryo-EM structure of human ABCA4 in NRPE-bound state
Method: EM (single particle) / Resolution: 3.4 Å

31002

7e7q

EMDB-31002, PDB-7e7q:
Cryo-EM structure of human ABCA4 in ATP-bound state
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

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

ChemComp-3PE:
1,2-Distearoyl-sn-glycerophosphoethanolamine / phospholipid*YM

ChemComp-HZL:
[(2S)-3-[2-[(E)-[(2E,4E,6E,8E)-3,7-dimethyl-9-(2,6,6-trimethylcyclohexen-1-yl)nona-2,4,6,8-tetraenylidene]amino]ethoxy-oxidanyl-phosphoryl]oxy-2-[(Z)-octadec-9-enoyl]oxy-propyl] (Z)-octadec-9-enoate

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

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsTRANSLOCASE / lipid transport / MEMBRANE PROTEIN

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