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From Proteopedia
Crystal Structure of Kinesin-3 KIF13B motor Y73C mutant
Structural highlights
FunctionPublication Abstract from PubMedProcessive kinesin motors contain a neck linker (NL) that mediates the chemo-mechanical coupling and controls the directionality and processivity. However, kinesin-3 NL remains poorly determined due to the lack of the structural information of the junction with the following neck coil (NC). Here, we determined the structure of the motor domain (MD)-NL-NCNT tandem of KIF13B that defines the junction between NL and NC and delineates kinesin-3 NL. Unexpectedly, the length of kinesin-3 NL is much shorter than the previously predicted one. In the MD-NL-NCNT structure, NL docks onto the MD with a conventional mode but the interaction between NL and the MD is relatively weak due to the shorter N-terminal cover strand of the MD. The optimal short NL and its weak interaction with the MD would generate the tight inter-head strain and facilitate the NL undocking, which may contribute to the fast and superprocessive motility of kinesin-3. Structural Delineation of the Neck Linker of Kinesin-3 for Processive Movement.,Ren J, Zhang Y, Wang S, Huo L, Lou J, Feng W J Mol Biol. 2018 May 9. pii: S0022-2836(18)30405-4. doi:, 10.1016/j.jmb.2018.05.010. PMID:29752968[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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