ATP synthases: bioinformatic based insights into how their electrochemically driven motor comprised of subunits a and c might serve as a drug target |
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Authors: | Masatomo Maeda |
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Institution: | (1) Department of Molecular Biology, School of Pharmaceutical Sciences, Iwate Medical University, Shiwa Iwate, 028-3694, Japan |
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Abstract: | ATP synthases, widely distributed in bacteria, eukaryotic mitochondria and chloroplasts, are highly conserved multi-subunit
complexes. Although the conserved acidic residue in the transmembrane helix of the c subunit functions in H+ transport, the surrounding residues differ among species. Such divergence could lead to different regulatory modes since
pH-dependent H+ transport has been demonstrated in E. coli with a c subunit carrying an additional acidic residue in the helix. There is further divergence in the number of c subunits that form the ring structure which is determined by the higher ordered structure. Recently, it was suggested that
certain chemicals recognize the a and c subunits of pathogenic bacterial F0. Since there may be structural divergence even in well-conserved ATP synthases, the c subunit-ring as well as the a subunit in F0 could be targets for drugs for specific bacterial species. |
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Keywords: | ATP synthase F0F1 c subunit a subunit Oxidative phosphorylation Proton transport Proton pump |
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