期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 19, 期 1, 页码 122-U149出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2190
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资金
- US National Institutes of Health, National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIH, NIAMS) [F32AR054653]
- NIH, National Institute of General Medical Sciences (NIGMS) [GM097079]
- NIH, NIGMS [GM-0080]
- US Department of Energy [DE-AC02-98CH10886]
Kinesins are molecular motors that require a divalent metal ion (for example, Mg2+) to convert the energy of ATP hydrolysis into directed force production along microtubules. Here we present the crystal structure of a recombinant kinesin motor domain bound to Mn2+ and ADP and report on a serine-to-cysteine substitution in the switch 1 motif of kinesin that allows its ATP hydrolysis activity to be controlled by adjusting the ratio of Mn2+ to Mg2+. This mutant kinesin binds ATP similarly in the presence of either metal ion, but its ATP hydrolysis activity is greatly diminished in the presence of Mg2+. In human kinesin-1 and kinesin-5 as well as Drosophila melanogaster kinesin-10 and kinesin-14, this defect is rescued by Mn2+, providing a way to control both the enzymatic activity and force-generating ability of these nanomachines.
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