Matches in SemOpenAlex for { <https://semopenalex.org/work/W2605989119> ?p ?o ?g. }
- W2605989119 abstract "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." @default.
- W2605989119 created "2017-04-28" @default.
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- W2605989119 date "2017-04-10" @default.
- W2605989119 modified "2023-10-02" @default.
- W2605989119 title "Crystal structure of Zen4 in the apo state reveals a missing conformation of kinesin" @default.
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- W2605989119 doi "https://doi.org/10.1038/ncomms14951" @default.
- W2605989119 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5394238" @default.
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- W2605989119 hasPublicationYear "2017" @default.
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