This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The goal of this project is to solve the structure of subunit 'a' of E.coli ATP Synthase. This is a membrane protein believed to be a part of the proton channel (Fo-complex). The attempts to solve the structure of the complete ATP Synthase or its membrane component by X-ray crystallography so far have not succeeded. We propose to use the structures of individual subunits of the Fo (a,b,c) complemented by the information on intersubunit contacts derived from chemical cross-linking in the native enzyme to elucidate the complete structure of the proton channel of ATP Synthase. The structures of the subunit c (Girvin et al., 1998) and of the membrane domain of the subunit b (Dmitriev et al., 1999) have been solved by NMR. Subunit a is the next challenge. This protein is presumed to be largely alpha-helical and is 271 amino acids long. We have developed a purification procedure and obtained good-quality 2D 15N,1H-chemical shift correlation spectra of the pure protein .
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