期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 15, 期 6, 页码 591-597出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1429
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资金
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [U54GM072970, R01GM033289, P01GM066275, T32GM008294] Funding Source: NIH RePORTER
- NIGMS NIH HHS [T32 GM008294, T32 GM008294-19, P01 GM066275-040006, R01 GM033289-21, T32 GM008294-11, P01 GM066275-030006, P01 GM066275, R01 GM033289-24, R01 GM033289-25, R01 GM033289-18, R01 GM033289-19, R01 GM033289, T32 GM008294-18, P01 GM066275-020006, P01 GM066275-050006, P01 GM066275-01A10006, T32 GM008294-15, R01 GM033289-16, T32 GM008294-13, R01 GM033289-20, GM33289, U54 GM072970, T32 GM008294-17, T32 GM008294-16, R01 GM033289-17, T32 GM008294-14, R01 GM033289-22, R01 GM033289-23, T32 GM008294-12] Funding Source: Medline
Myosin VI has challenged the lever arm hypothesis of myosin movement because of its ability to take similar to 36-nm steps along actin with a canonical lever arm that seems to be too short to allow such large steps. Here we demonstrate that the large step of dimeric myosin VI is primarily made possible by a medial tail in each monomer that forms a rare single alpha-helix of similar to 10 nm, which is anchored to the calmodulin-bound IQ domain by a globular proximal tail. With the medial tail contributing to the similar to 36-nm step, rather than dimerizing as previously proposed, we show that the cargo binding domain is the dimerization interface. Furthermore, the cargo binding domain seems to be folded back in the presence of the catalytic head, constituting a potential regulatory mechanism that inhibits dimerization.
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