Identification of residues defining phospholipid flippase substrate specificity of type IV P-type ATPases

Type IV P-type ATPases (P4-ATPases) catalyze translocation of phospholipid across a membrane to establish an asymmetric bilayer structure with phosphatidylserine (PS) and phosphatidylethanolamine (PE) restricted to the cytosolic leaflet. The mechanism for how P4-ATPases recognize and flip phospholip...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2012-02, Vol.109 (6), p.1822-1823
Hauptverfasser:	Baldridge, Ryan D., Graham, Todd R.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine triphosphatase Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - metabolism Amino Acid Sequence Amino Acid Substitution Amino Acids - metabolism ATP-Binding Cassette Transporters - chemistry ATP-Binding Cassette Transporters - metabolism Binding sites Biological Sciences Calcium-Transporting ATPases - chemistry Calcium-Transporting ATPases - metabolism Cell Membrane - enzymology Endoplasmic Reticulum - metabolism Green Fluorescent Proteins - metabolism Lipids Membrane Transport Proteins - metabolism Models, Molecular Molecular Sequence Data Mutant Proteins - chemistry Mutant Proteins - metabolism Phosphatidylcholines - metabolism Phosphatidylethanolamines - metabolism Phosphatidylserines - metabolism Phospholipid Transfer Proteins - chemistry Phospholipid Transfer Proteins - metabolism PNAS Plus PNAS PLUS (AUTHOR SUMMARIES) Protein Structure, Tertiary Protein Transport Proteins Recombinant Proteins - metabolism Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism Signal transduction Structure-Activity Relationship Substrate Specificity
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