3U06

Crystal structure of the kinesin-14 NcdG347D

Summary for 3U06

• Entry DOI: 10.2210/pdb3u06/pdb
• Descriptor: Protein claret segregational, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: motor domain, stalk rotation, power stroke, kinesin-14, microtubule binding, ncd, transport, molecular motor, cell division, atp binding, microtubules, motor protein
• Biological source: Drosophila melanogaster (Fruit fly)
• Cellular location: Cytoplasm, cytoskeleton : P20480
• Total number of polymer chains: 2
• Total formula weight: 94920.75

Authors

Liu, H.-L.,Pemble IV, C.W.,Endow, S.A. (deposition date: 2011-09-28, release date: 2012-03-07, Last modification date: 2024-02-28)

Primary citation

Liu, H.L.,Pemble Iv, C.W.,Endow, S.A.
Neck-motor interactions trigger rotation of the kinesin stalk.
Sci Rep, 2:236-236, 2012

PubMed Abstract: Rotation of the coiled-coil stalk of the kinesin-14 motors is thought to drive displacements or steps by the motor along microtubules, but the structural changes that trigger stalk rotation and the nucleotide state in which it occurs are not certain. Here we report a kinesin-14 neck mutant that releases ADP more slowly than wild type and shows weaker microtubule affinity, consistent with defective stalk rotation. Unexpectedly, crystal structures show the stalk fully rotated - neck-motor interactions destabilize the stalk, causing it to rotate and ADP to be released, and alter motor affinity for microtubules. A new structural pathway accounts for the coupling of stalk rotation - the force-producing stroke - to changes in motor affinity for nucleotide and microtubules. Sequential disruption of salt bridges that stabilize the unrotated stalk could cause the stalk to initiate and complete rotation in different nucleotide states.

PubMed: 22355749
DOI: 10.1038/srep00236

Experimental method

X-RAY DIFFRACTION (2.35 Å)