Visualization of a peripheral stalk in V-type ATPase: Evidence for the stator structure essential to rotational catalysis

被引:88
作者
Boekema, EJ
Ubbink-Kok, T
Lolkema, JS
Brisson, A
Konings, WN
机构
[1] Univ Groningen, Dept Biophys Chem, Groningen Biomol Sci & Biotechnol Inst, NL-9747 AG Groningen, Netherlands
[2] Univ Groningen, Dept Microbiol, Groningen Biomol Sci & Biotechnol Inst, NL-9751 NN Haren, Netherlands
关键词
D O I
10.1073/pnas.94.26.14291
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
F- and V-type ATPases are central enzymes in energy metabolism that couple synthesis or hydrolysis of ATP to the translocation of H+ or Na+ across biological membranes. They consist of a soluble headpiece that contains the catalytic sites and an integral membrane-bound part that conducts the ion flow. Energy coupling is thought to occur through the physical rotation of a stalk that connects the two parts of the enzyme complex. This mechanism implies that a stator-like structure prevents the rotation of the headpiece relative to the membrane-bound part. Such a structure has not been observed to date. Here, we report the projected structure of the V-type Na+-ATPase of Clostridium fervidus as determined by electron microscopy. Besides the central stalk, a second stalk of 130 Angstrom in length is observed that connects the headpiece and membrane-bound part in the periphery of the complex. This additional stalk is likely to be the stator.
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页码:14291 / 14293
页数:3
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