[H(+)-transporting ATP synthases: insights into how their electrochemically driven motor might serve as a drug target].
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 proton transport, the surrounding residues differ among species. Such divergence could lead to different regulatory modes since pH-dependent proton transport has been demonstrated in Escherichia 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 in F(0). Recently, it was also suggested that certain chemicals recognize the a and c subunits of pathogenic bacterial F(0). Since there may be structural divergence even in well-conserved ATP synthases, the c subunit-ring as well as the a subunit in F(0) could be targets for drugs for specific bacterial species.
Maeda
Masatomo
M
Department of Molecular Biology, School of Pharmacy, Iwate Medical University, Iwate, Japan. mmaeda@iwate-med.ac.jp
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents; D025243:Bacterial Proton-Translocating ATPases; D015195:Drug Design; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics / Q000378:metabolism; D029968:Escherichia coli Proteins; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000502:physiology
D000900:Anti-Bacterial Agents; D029968:Escherichia coli Proteins; C523987:ATP synthase subunit c, E coli; D025243:Bacterial Proton-Translocating ATPases; D006180:Proton-Translocating ATPases; C074428:atpB protein, E coli