Neck rotation and neck mimic docking in the noncatalytic Kar3-associated protein Vik1.

ABSTRACT:

Background

Kar3Vik1 is a heterodimeric kinesin with one catalytic subunit (Kar3) and one noncatalytic subunit (Vik1).

Results

Vik1 experiences conformational changes in regions analogous to the force-producing elements in catalytic kinesins.

Conclusion

A molecular mechanism by which Kar3 could trigger Vik1's release from microtubules was revealed.

Significance

These findings will serve as the prototype for understanding the motile mechanism of kinesin-14 motors in general. It is widely accepted that movement of kinesin motor proteins is accomplished by coupling ATP binding, hydrolysis, and product release to conformational changes in the microtubule-binding and force-generating elements of their motor domain. Therefore, understanding how the Saccharomyces cerev

SUBMITTER: Duan D 

PROVIDER: S-EPMC3504745 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature