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Structure and multistate function of the transmembrane electron transporter CcdA.
Williamson, Jessica A; Cho, Seung-Hyun; Ye, Jiqing; Collet, Jean-Francois; Beckwith, Jonathan R; Chou, James J.
Afiliación
  • Williamson JA; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, USA.
  • Cho SH; WELBIO, Brussels, Belgium.
  • Ye J; Department of Microbiology and Immunobiology, Harvard Medical School, Boston, Massachusetts, USA.
  • Collet JF; de Duve Institute, Université Catholique de Louvain, Brussels, Belgium.
  • Beckwith JR; Department of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA.
  • Chou JJ; WELBIO, Brussels, Belgium.
Nat Struct Mol Biol ; 22(10): 809-14, 2015 Oct.
Article en En | MEDLINE | ID: mdl-26389738
The mechanism by which transmembrane reductases use a single pair of cysteine residues to relay electrons between protein substrates across biological membranes is a long-standing mystery in thiol-redox biochemistry. Here we show the NMR structure of a reduced-state mimic of archaeal CcdA, a protein that transfers electrons across the inner membrane, by using a redox-active NMR sample. The two cysteine positions in CcdA are separated by 20 Å. Whereas one is accessible to the cytoplasm, the other resides in the protein core, thus implying that conformational exchange is required for periplasmic accessibility. In vivo mixed disulfide-trapping experiments validated the functional positioning of the cysteines, and in vitro accessibility results confirmed conformational exchange. Our NMR and functional data together show the existence of multiple conformational states and suggest a four-state model for relaying electrons from cytosolic to periplasmic redox substrates.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Oxidorreductasas / Proteínas Portadoras / Modelos Moleculares / Proteínas Arqueales / Proteínas de la Membrana Idioma: En Revista: Nat Struct Mol Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2015 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Oxidorreductasas / Proteínas Portadoras / Modelos Moleculares / Proteínas Arqueales / Proteínas de la Membrana Idioma: En Revista: Nat Struct Mol Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2015 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos