Directed evolution of a sphingomyelin flippase reveals mechanism of substrate backbone discrimination by a P4-ATPase.

Roland, Bartholomew P; Graham, Todd R

Roland, Bartholomew P; Graham, Todd R.

Affiliation

Roland BP; Department of Biological Sciences, Vanderbilt University, Nashville, TN 37235.
Graham TR; Department of Biological Sciences, Vanderbilt University, Nashville, TN 37235 tr.graham@vanderbilt.edu.

Proc Natl Acad Sci U S A ; 113(31): E4460-6, 2016 08 02.

Article in En | MEDLINE | ID: mdl-27432949

Subject(s)

ATP-Binding Cassette Transporters/genetics; Adenosine Triphosphatases/genetics; Gain of Function Mutation; Saccharomyces cerevisiae Proteins/genetics; Saccharomyces cerevisiae/genetics; Sphingomyelins/metabolism; ATP-Binding Cassette Transporters/metabolism; Adenosine Triphosphatases/metabolism; Amino Acid Sequence; Asparagine/genetics; Asparagine/metabolism; Biological Transport/genetics; Cell Membrane/metabolism; Directed Molecular Evolution; Mutagenesis; Saccharomyces cerevisiae/enzymology; Saccharomyces cerevisiae Proteins/metabolism; Sequence Homology, Amino Acid; Substrate Specificity

Key words

P4-ATPase; directed evolution; membrane asymmetry; sphingomyelin

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Full text: 1 Database: MEDLINE Main subject: Saccharomyces cerevisiae / Sphingomyelins / Adenosine Triphosphatases / ATP-Binding Cassette Transporters / Saccharomyces cerevisiae Proteins / Gain of Function Mutation Type of study: Prognostic_studies Language: En Year: 2016 Type: Article

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