Ca2+ ATPase Conformational Transitions in Lipid Bilayers Mapped by Site-directed Ethylation and Solid-State NMR
作者： Vitaly V. Vostrikov , Martin Gustavsson , Tata Gopinath , Dan Mullen , Alysha A. Dicke
DOI: 10.1021/ACSCHEMBIO.5B00953
关键词:
摘要: To transmit signals across cellular compartments, many membrane-embedded enzymes undergo extensive conformational rearrangements. Monitoring these events in lipid bilayers by NMR at atomic resolution has been challenging due to the large size of systems. It is further exacerbated for mammalian proteins that are difficult express and label with NMR-active isotopes. Here, we synthesized engineered 13C ethyl groups on native cysteines map structural transitions sarcoplasmic reticulum Ca2+-ATPase, a 110 kDa transmembrane enzyme transports Ca2+ into reticulum. Using magic angle spinning NMR, monitored chemical shifts methylene methyl derivatized cysteine residues along major steps enzymatic cycle. The sensitive ATPase changes induced upon nucleotide ion binding ideal probes active inactive states enzyme. This new approach extend...
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