The RCK domain of the KtrAB K+ transporter:: Multiple conformations of an octameric ring

被引:78
作者
Albright, Ronald A.
Ibar, Jose-Luis Vaquez
Kim, Chae Un
Gruner, Soi M.
Morais-Cabral, Joao Henrique
机构
[1] Yale Univ, Dept Mol Biophys & Biochem, New Haven, CT 06520 USA
[2] Cornell Univ, Cornell High Energy Synchrotron Source, Ithaca, NY 14853 USA
[3] Cornell Univ, Dept Phys, Ithaca, NY 14853 USA
关键词
D O I
10.1016/j.cell.2006.08.028
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要
The KtrAB ion transporter is a complex of the KtrB membrane protein and KtrA, an RCK domain. RCK domains regulate eukaryotic and prokaryotic membrane proteins involved in K+ transport. Conflicting functional models have proposed two different oligomeric arrangements for RCK domains, tetramer versus octamer. Our results for the KtrAB RCK domain clearly show an octamer in solution and in the crystal. We determined the structure of this protein in three different octameric ring conformations that resemble the RCK-domain octamer observed in the MthK potassium channel but show striking differences in size and symmetry. We present experimental evidence for the association between one RCK octameric ring and two KtrB membrane proteins. These results provide insights into the quaternary organization of the KtrAB transporter and its mechanism of activation and show that the RCK-domain octameric ring model is generally applicable to other ion-transport systems.
引用
收藏
页码:1147 / 1159
页数:13
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