Chapter title |
The Use of Metal Fluoride Compounds as Phosphate Analogs for Understanding the Structural Mechanism in P-type ATPases
|
---|---|
Chapter number | 19 |
Book title |
P-Type ATPases
|
Published in |
Methods in molecular biology, January 2016
|
DOI | 10.1007/978-1-4939-3179-8_19 |
Pubmed ID | |
Book ISBNs |
978-1-4939-3178-1, 978-1-4939-3179-8
|
Authors |
Stefania J. Danko, Hiroshi Suzuki |
Abstract |
The membrane-bound protein family, P-type ATPases, couples ATP hydrolysis with substrate transport across the membrane and forms an obligatory auto-phosphorylated intermediate in the transport cycle. The metal fluoride compounds, BeF x , AlF x , and MgF x , as phosphate analogs stabilize different enzyme structural states in the phosphoryl transfer/hydrolysis reactions, thereby fixing otherwise short-lived intermediate and transient structural states and enabling their biochemical and atomic-level crystallographic studies. The compounds thus make an essential contribution for understanding of the ATP-driven transport mechanism. Here, with a representative member of P-type ATPase, sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA), we describe the method for their binding and for structural and functional characterization of the bound states, and their assignments to states occurring in the transport cycle. |
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Demographic breakdown
Readers by professional status | Count | As % |
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Student > Master | 3 | 38% |
Unspecified | 1 | 13% |
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Student > Ph. D. Student | 1 | 13% |
Unknown | 2 | 25% |
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Unspecified | 1 | 13% |
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Unknown | 2 | 25% |