@article {Preiss:2014:0950-382X:973,
title = "The cring ion binding site of the ATP synthase from Bacillus pseudofirmusOF4 is adapted to alkaliphilic lifestyle",
journal = "Molecular Microbiology",
parent_itemid = "infobike://bsc/mole",
publishercode ="bp",
year = "2014",
volume = "92",
number = "5",
publication date ="2014-06-01T00:00:00",
pages = "973-984",
itemtype = "ARTICLE",
issn = "0950-382X",
eissn = "1365-2958",
url = "https://www.ingentaconnect.com/content/bsc/mole/2014/00000092/00000005/art00007",
doi = "doi:10.1111/mmi.12605",
author = "Preiss, Laura and Langer, Julian D. and Hicks, David B. and Liu, Jun and Yildiz, {\"O}zkan and Krulwich, Terry A. and Meier, Thomas",
abstract = "In the cring rotor of ATP synthases ions are shuttled across the membrane during ATP synthesis by a unique rotary mechanism. We investigated characteristics of the cring from the alkaliphile B
acillus pseudofirmusOF4 with respect to evolutionary
adaptations to operate with protons at high environmental pH. The Xray structures of the wildtype c13 ring at pH 9.0 and a neutralophilelike mutant (P51A) at pH 4.4, at 2.4 and 2.8 \AA resolution, respectively, reveal a dependency of the
conformation and protonation state of the protonbinding glutamate (E54) on environmental hydrophobicity. Faster labelling kinetics with the inhibitor dicyclohexylcarbodiimide (DCCD) demonstrate a greater flexibility of E54 in the mutant due to reduced water occupancy
within the H+ binding site. A second neutralophilelike mutant (V21N) shows reduced growth at high pH, which is explained by restricted conformational freedom of the mutant's E54 carboxylate. The study directly connects subtle structural adaptations
of the cring ion binding site to in vivo effects of alkaliphile cell physiology.",
}