In this section
@article{Meier:2005:10.1126/science.1111199,
author = {Meier, T and Polzer, P and Diederichs, K and Welte, W and Dimroth, P},
doi = {10.1126/science.1111199},
journal = {Science},
pages = {659--662},
title = {Structure of the Rotor Ring of F-Type Na <sup>+</sup> -ATPase from <i>Ilyobacter tartaricus</i>},
url = {http://dx.doi.org/10.1126/science.1111199},
volume = {308},
year = {2005}
}
TY - JOUR
AB - <jats:p> In the crystal structure of the membrane-embedded rotor ring of the sodium ion–translocating adenosine 5′-triphosphate (ATP) synthase of <jats:italic>Ilyobacter tartaricus</jats:italic> at 2.4 angstrom resolution, 11 c subunits are assembled into an hourglass-shaped cylinder with 11-fold symmetry. Sodium ions are bound in a locked conformation close to the outer surface of the cylinder near the middle of the membrane. The structure supports an ion-translocation mechanism in the intact ATP synthase in which the binding site converts from the locked conformation into one that opens toward subunit a as the rotor ring moves through the subunit a/c interface. </jats:p>
AU - Meier,T
AU - Polzer,P
AU - Diederichs,K
AU - Welte,W
AU - Dimroth,P
DO - 10.1126/science.1111199
EP - 662
PY - 2005///
SN - 0036-8075
SP - 659
TI - Structure of the Rotor Ring of F-Type Na <sup>+</sup> -ATPase from <i>Ilyobacter tartaricus</i>
T2 - Science
UR - http://dx.doi.org/10.1126/science.1111199
UR - https://doi.org/10.1126/science.1111199
VL - 308
ER -
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