5x3e

Publication Abstract from PubMed

Kinesins hydrolyse ATP to transport intracellular cargoes along microtubules. Kinesin neck linker (NL) functions as the central mechano-chemical coupling element by changing its conformation through the ATPase cycle. Here we report the crystal structure of kinesin-6 Zen4 in a nucleotide-free, apo state, with the NL initial segment (NIS) adopting a backward-docked conformation and the preceding alpha6 helix partially melted. Single-molecule fluorescence resonance energy transfer (smFRET) analyses indicate the NIS of kinesin-1 undergoes similar conformational changes under tension in the two-head bound (2HB) state, whereas it is largely disordered without tension. The backward-docked structure of NIS is essential for motility of the motor. Our findings reveal a key missing conformation of kinesins, which provides the structural basis of the stable 2HB state and offers a tension-based rationale for an optimal NL length to ensure processivity of the motor.

Crystal structure of Zen4 in the apo state reveals a missing conformation of kinesin.,Guan R, Zhang L, Su QP, Mickolajczyk KJ, Chen GY, Hancock WO, Sun Y, Zhao Y, Chen Z Nat Commun. 2017 Apr 10;8:14951. doi: 10.1038/ncomms14951. PMID:28393873^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.