Mutations Define Cross-talk between the N-terminal Nucleotide-binding Domain and Transmembrane Helix-2 of the Yeast Multidrug Transporter Pdr5: POSSIBLE CONSERVATION OF A SIGNALING INTERFACE FOR COUPLING ATP HYDROLYSIS TO DRUG TRANSPORT

The yeast Pdr5 multidrug transporter is an important member of the ATP-binding cassette superfamily of proteins. We describe a novel mutation (S558Y) in transmembrane helix 2 of Pdr5 identified in a screen for suppressors that eliminated Pdr5-mediated cycloheximide hyper-resistance. Nucleotides as w...

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Main Authors: Sauna, Zuben E., Bohn, Sherry Supernavage, Rutledge, Robert, Dougherty, Michael P., Cronin, Susan, May, Leopold, Xia, Di, Ambudkar, Suresh V., Golin, John
Formato: Artigo
Idioma:Inglês
Publicado em: American Society for Biochemistry and Molecular Biology 2008
Assuntos:
Membrane Transport, Structure, Function, and Biogenesis
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2596398/
https://ncbi.nlm.nih.gov/pubmed/18842589
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M806446200
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