ATP synthases: bioinformatic based insights into how their electrochemically driven motor comprised of subunits a and c might serve as a drug target.

Journal of Bioenergetics and Biomembranes
Masatomo Maeda

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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Citations

Feb 2, 2010·Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan·Masatomo Maeda
Mar 3, 2010·Biochimica Et Biophysica Acta·David B HicksTerry A Krulwich
Jul 4, 2019·SLAS Discovery·Salvatore NesciAlessandra Pagliarani
Oct 6, 2018·Scientific Reports·Chen XuZhi Ming He

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