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  The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic lifestyle

Preiss, L., Langer, J. D., Hicks, D. B., Liu, J., Yildiz, Ö., Krulwich, T. A., et al. (2014). The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic lifestyle. Molecular Microbiology, 92(5), 973-984. doi:10.1111/mmi.12605.

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 Creators:
Preiss, Laura1, Author           
Langer, Julian David2, Author           
Hicks, David B.3, Author
Liu, Jun3, Author
Yildiz, Özkan1, Author           
Krulwich, Terry A.3, Author
Meier, Thomas1, Author           
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
2Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
3External Organizations, ou_persistent22              

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Free keywords: ATP synthase
 Abstract: In the c-ring rotor of ATP synthases ions are shuttled across the membrane during ATP synthesis by a unique rotary mechanism. We investigated characteristics of the c-ring from the alkaliphile Bacillus pseudofirmus OF4 with respect to evolutionary adaptations to operate with protons at high environmental pH. The X-ray structures of the wild-type c13 ring at pH 9.0 and a 'neutralophile-like' mutant (P51A) at pH 4.4, at 2.4 and 2.8 Å resolution, respectively, reveal a dependency of the conformation and protonation state of the proton-binding glutamate (E(54) ) on environmental hydrophobicity. Faster labelling kinetics with the inhibitor dicyclohexylcarbodiimide (DCCD) demonstrate a greater flexibility of E(54) in the mutant due to reduced water occupancy within the H(+) binding site. A second 'neutralophile-like' mutant (V21N) shows reduced growth at high pH, which is explained by restricted conformational freedom of the mutant's E(54) carboxylate. The study directly connects subtle structural adaptations of the c-ring ion binding site to in vivo effects of alkaliphile cell physiology.

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Language(s): eng - English
 Dates: 2014-04-242014-06
 Publication Status: Published in print
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 695676
DOI: 10.1111/mmi.12605
 Degree: -

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Title: Molecular Microbiology
  Other : Mol. Microbiol.
Source Genre: Journal
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Publ. Info: Wiley
Pages: - Volume / Issue: 92 (5) Sequence Number: - Start / End Page: 973 - 984 Identifier: ISSN: 0950-382X
CoNE: https://pure.mpg.de/cone/journals/resource/954925574950