Structure and Function of the Vacuolar H+-ATPase: Moving from Low-Resolution Models to High-Resolution Structures |
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Authors: | Michael Harrison Lyndsey Durose Chun Feng Song Elizabeth Barratt John Trinick Richard Jones John B. C. Findlay |
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Affiliation: | (1) School of Biochemistry and Molecular Biology, University of Leeds, Leeds, LS2 9JT, United Kingdom;(2) School of Biomedical Sciences, University of Leeds, Leeds, United Kingdom |
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Abstract: | In the absence of a high-resolution structure for the vacuolar H+-ATPase, a number of approaches can yield valuable information about structure/function relationships in the enzyme. Electron microscopy can provide not only a representation of the overall architecture of the complex, but also a low-resolution map onto which structures solved for individually expressed subunits can be fitted. Here we review the possibilities for electron microscopy of the Saccharomyces V-ATPase and examine the suitability of V-ATPase subunits for expression in high yield prokaryotic systems, a key step towards high-resolution structural studies. We also review the role of experimentally-derived structural models in understanding structure/function relationships in the V-ATPase, with particular reference to the complex of proton-translocating 16 kDa proteolipids in the membrane domain of the V-ATPase. This model in turn makes testable predictions about the sites of binding of bafilomycins and the functional interactions between the proteolipid and the single-copy membrane subunit Vph1p, with implications for the constitution of the proton translocation pathway. |
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Keywords: | Vacuolar membrane V-ATPase expression circular dichroism electron microscopy modelling |
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