5X3E

kinesin 6

Summary for 5X3E

• Entry DOI: 10.2210/pdb5x3e/pdb
• Descriptor: Kinesin-like protein, SULFATE ION, IODIDE ION, ... (4 entities in total)
• Functional Keywords: kinesin 6, apo state, neck linker, motor protein
• Biological source: Caenorhabditis elegans
• Total number of polymer chains: 2
• Total formula weight: 106165.79

Authors

Chen, Z.,Guan, R.,Zhang, L. (deposition date: 2017-02-04, release date: 2017-04-19, Last modification date: 2024-03-27)

Primary citation

Guan, R.,Zhang, L.,Su, Q.P.,Mickolajczyk, K.J.,Chen, G.Y.,Hancock, W.O.,Sun, Y.,Zhao, Y.,Chen, Z.
Crystal structure of Zen4 in the apo state reveals a missing conformation of kinesin
Nat Commun, 8:14951-14951, 2017

PubMed Abstract: 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 α6 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.

PubMed: 28393873
DOI: 10.1038/ncomms14951

Experimental method

X-RAY DIFFRACTION (2.61 Å)