Structural investigations of the membrane-embedded rotor ring of the F-ATPase from Clostridium paradoxum

被引：48
作者：
Meier, Thomas
Ferguson, Scott A.
Cook, Gregory M.
Dimroth, Peter
Vonck, Janet
机构：
[1] Max Planck Inst Biophys, D-60438 Frankfurt, Germany
[2] ETH, Inst Mikrobiol, CH-8093 Zurich, Switzerland
[3] Univ Otago, Otago Sch Med Sci, Dept Microbiol & Immunol, Dunedin, New Zealand
来源：
JOURNAL OF BACTERIOLOGY | 2006年 / 188卷 / 22期
关键词：
D O I：
10.1128/JB.00934-06
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
The Na+-translocating F-ATPase of the thermoalkaliphilic bacterium Clostridium paradoxum harbors an oligomeric ring of c subunits that resists dissociation by sodium dodecyl sulfate. The c ring has been isolated and crystallized in two dimensions. From electron microscopy of these c-ring crystals, a projection map was calculated to 7 angstrom resolution. In the projection map, each c ring consists of two concentric, slightly staggered, packed rings, each composed of 11 densities representing the alpha-helices. On the basis of these results, it was determined that the F-ATPase from C paradoxum contains an undecameric c ring.
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页码：7759 / 7764
页数：6
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