Subunit F of A-ATP synthases is an ATPase stimulating subunit
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چکیده
منابع مشابه
A novel subunit of vacuolar H(+)-ATPase related to the b subunit of F-ATPases.
The subunit structure of the vacuolar H(+)-ATPase (V-ATPase) membrane sector is not entirely known. The proteolipid is the only subunit that has been implicated in the mechanism of energy transfer in the enzyme. We have identified a protein (M16) that co-purifies with the V-ATPase complex from bovine chromaffin granules. Information obtained from the amino acid sequence of a proteolytic fragmen...
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Subunit I of chloroplast ATP synthase is reviewed until now to be equivalent to subunit b of Escherichia coli ATP synthase, whereas subunit II is suggested to be an additional subunit in photosynthetic ATP synthases lacking a counterpart in E. coli. After publication of some sequences of subunits II a revision of this assignment is necessary. Based on the analysis of 51 amino acid sequences of ...
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The tuberculosis drug bedaquiline inhibits mycobacterial F-ATP synthase by binding to its c subunit. Using the purified ε subunit of the synthase and spectroscopy, we previously demonstrated that the drug interacts with this protein near its unique tryptophan residue. Here, we show that replacement of ε's tryptophan with alanine resulted in bedaquiline hypersusceptibility of the bacteria. Overe...
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Subunit movements within the H(+)-ATP synthase from chloroplasts (CF(0)F(1)) are investigated during ATP synthesis. The gamma-subunit (gammaCys-322) is covalently labeled with a fluorescence donor (ATTO532). A fluorescence acceptor (adenosine 5'-(beta,gamma-imino)triphosphate (AMPPNP)-ATTO665) is noncovalently bound to a noncatalytic site at one alpha-subunit. The labeled CF(0)F(1) is integrate...
متن کاملF1-ATPase, the C-terminal End of Subunit Is Not Required for ATP Hydrolysis-driven Rotation*
ATP hydrolysis by the isolated F1-ATPase drives the rotation of the central shaft, subunit , which is located within a hexagon formed by subunits ( )3. The C-terminal end of forms an -helix which properly fits into the “hydrophobic bearing” provided by loops of subunits and . This “bearing” is expected to be essential for the rotary function. We checked the importance of this contact region by ...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Bioenergetics
سال: 2014
ISSN: 0005-2728
DOI: 10.1016/j.bbabio.2014.05.217