Quaternary structure of V1 and F1 ATPase: significance of structural homologies and diversities.
Quaternary structure of V1 and F1 ATPase: significance of structural homologies and diversities.
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V1 和 F1 ATP 酶的四级结构：结构同源性和多样性的意义。
DOI：
10.1021/bi982367a
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发表时间：
1998
期刊：
影响因子：
2.9
通讯作者：
G. Grüber
中科院分区：
文献类型：
--
作者：
D. Svergun;S. Konrad;M. Huss;M. Koch;H. Wieczorek;K. Altendorf;V. Volkov;G. Grüber
利用小角X射线散射（SAXS）对烟草天蛾（Manducasexta）V1 ATPase和大肠杆菌（Escherichiacoli）F1 ATPase进行了表征。配合物的回转半径（Rg）分别为6.2 +/- 0.1和4.7 +/-0.02nm。M. sexta V1 ATP酶从头开始测定散射数据显示6个质量，推测为A和B亚基，以交替的方式围绕3倍轴排列。长度为约11.0 nm的第七质量垂直于六聚体单元的中心延伸。这个中心物质被认为是完整的V1 V（O）-ATP酶中连接V1和膜结构域（V（O））的柄。相比之下，E.大肠杆菌具有一个准三重对称的主要部分的酶。结构的总体不对称性由茎给出，假设包括中心茎亚基。V_1和F_1 ATP酶的特征揭示了复合物中关键组分的结构同源性和差异性。
The V1 ATPase from the tobacco hornworm Manduca sexta and the Escherichia coli F1 ATPase were characterized by small-angle X-ray scattering (SAXS). The radii of gyration (Rg) of the complexes were 6.2 +/- 0.1 and 4.7 +/- 0.02 nm, respectively. The shape of the M. sexta V1 ATPase was determined ab initio from the scattering data showing six masses, presumed to be the A and B subunits, arranged in an alternating manner about a 3-fold axis. A seventh mass with a length of about 11.0 nm extends perpendicularly to the center of the hexameric unit. This central mass is presumed to be the stalk that connects V1 with the membrane domain (V(O)) in the intact V1V(O)-ATPase. In comparison, the shape of the F1 ATPase from E. coli possesses a quasi-3-fold symmetry over the major part of the enzyme. The overall asymmetry of the structure is given by a stem, assumed to include the central stalk subunits. The features of the V1 and F1 ATPase reveal structural homologies and diversities of the key components of the complexes.