kinesin 6kinesin 6

Structural highlights

5x3e is a 2 chain structure with sequence from Caeel. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Gene:zen-4, CELE_M03D4.1, M03D4.1 (CAEEL)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

See Also

References

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

5x3e, resolution 2.61Å

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