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TitleMolecular organization and ATP-induced conformational changes of ABCA4, the photoreceptor-specific ABC transporter.
Journal, issue, pagesStructure, Vol. 21, Issue 5, Page 854-860, Year 2013
Publish dateMay 7, 2013
AuthorsYaroslav Tsybovsky / Tivadar Orban / Robert S Molday / Derek Taylor / Krzysztof Palczewski /
PubMed AbstractATP-binding cassette (ABC) transporters use ATP to translocate various substrates across cellular membranes. Several members of subfamily A of mammalian ABC transporters are associated with severe ...ATP-binding cassette (ABC) transporters use ATP to translocate various substrates across cellular membranes. Several members of subfamily A of mammalian ABC transporters are associated with severe health disorders, but their unusual complexity and large size have so far precluded structural characterization. ABCA4 is localized to the discs of vertebrate photoreceptor outer segments. This protein transports N-retinylidene-phosphatidylethanolamine to the outer side of disc membranes to prevent formation of toxic compounds causing macular degeneration. An 18 Å-resolution structure of ABCA4 isolated from bovine rod outer segments was determined using electron microscopy and single-particle reconstruction. Significant conformational changes in the cytoplasmic and transmembrane regions were observed upon binding of a nonhydrolyzable ATP analog and accompanied by altered hydrogen/deuterium exchange in the Walker A motif of one of the nucleotide-binding domains. These findings provide an initial view of the molecular organization and functional rearrangements for any member of the ABCA subfamily of ABC transporters.
External linksStructure / PubMed:23562398 / PubMed Central
MethodsEM (single particle)
Resolution18.1 - 18.9 Å
Structure data

EMDB-5497:
Structure of ABCA4, the photoreceptor-specific ATP-binding cassette transporter
Method: EM (single particle) / Resolution: 18.1 Å

EMDB-5498:
Structure of ABCA4, the photoreceptor-specific ATP-binding cassette transporter, in complex with AMPPNP
Method: EM (single particle) / Resolution: 18.9 Å

Source
  • Bos taurus (cattle)

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