3U06

Crystal structure of the kinesin-14 NcdG347D

3U06 の概要

• エントリーDOI: 10.2210/pdb3u06/pdb
• 分子名称: Protein claret segregational, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: motor domain, stalk rotation, power stroke, kinesin-14, microtubule binding, ncd, transport, molecular motor, cell division, atp binding, microtubules, motor protein
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• 細胞内の位置: Cytoplasm, cytoskeleton : P20480
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 94920.75

構造登録者

Liu, H.-L.,Pemble IV, C.W.,Endow, S.A. (登録日: 2011-09-28, 公開日: 2012-03-07, 最終更新日: 2024-02-28)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.35 Å)