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-Structure paper
タイトル | Molecular organization and ATP-induced conformational changes of ABCA4, the photoreceptor-specific ABC transporter. |
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ジャーナル・号・ページ | Structure, Vol. 21, Issue 5, Page 854-860, Year 2013 |
掲載日 | 2013年5月7日 |
著者 | Yaroslav Tsybovsky / Tivadar Orban / Robert S Molday / Derek Taylor / Krzysztof Palczewski / |
PubMed 要旨 | 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 ...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. |
リンク | Structure / PubMed:23562398 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 18.1 - 18.9 Å |
構造データ | EMDB-5497: EMDB-5498: |
由来 |
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