Molecular architecture of the undecameric rotor of a bacterial Na+-ATP synthase.
Molecular architecture of the undecameric rotor of a bacterial Na+-ATP synthase.
复制标题
细菌 Na -ATP 合酶十一聚体转子的分子结构。
DOI:
10.1016/s0022-2836(02)00597-1
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发表时间:
2002
影响因子:
5.6
通讯作者:
P. Dimroth
中科院分区:
文献类型:
--
作者:
J. Vonck;Tassilo Krug von Nidda;T. Meier;U. Matthey;D. Mills;W. Kühlbrandt;P. Dimroth
The sodium ion-translocating F1F0ATP synthase from the bacterium Ilyobacter tartaricus contains a remarkably stable rotor ring composed of 11 c subunits. The rotor ring was isolated, crystallised in two dimensions and analysed by electron cryo-microscopy. Here, we present an α-carbon model of the c-subunit ring. Each monomeric c subunit of 89 amino acid residues folds into a helical hairpin consisting of two membrane-spanning helices and a cytoplasmic loop. The 11 N-terminal helices are closely spaced within an inner ring surrounding a cavity of ∼17Å (1.7nm). The tight helix packing leaves no space for side-chains and is accounted for by a highly conserved motif of four glycine residues in the inner, N-terminal helix. Each inner helix is connected by a clearly visible loop to an outer C-terminal helix. The outer helix has a kink near the position of the ion-binding site residue Glu65 in the centre of the membrane and another kink near the C terminus. Two helices from the outer ring and one from the inner ring form the ion-binding site in the middle of the membrane and a potential access channel from the binding site to the cytoplasmic surface. Three possible inter-subunit ion-bridges are likely to account for the remarkable temperature stability of I.tartaricus c-rings compared to those of other organisms.
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影响因子:
5.6
作者:
Luecke, H;Schobert, B;Lanyi, JK
通讯作者:
Lanyi, JK
DOI:
10.1073/pnas.96.14.7785
发表时间:
1999-07-06
影响因子:
11.1
作者:
Dmitriev, OY;Jones, PC;Fillingame, RH
通讯作者:
Fillingame, RH
影响因子:
2.9
作者:
Girvin, ME;Rastogi, VK;Fillingame, RH
通讯作者:
Fillingame, RH
影响因子:
5.6
作者:
HENDERSON, R;BALDWIN, JM;DOWNING, KH
通讯作者:
DOWNING, KH