7S5U

Extended bipolar assembly domain of kinesin-5 minifilament

Summary for 7S5U

• Entry DOI: 10.2210/pdb7s5u/pdb
• Descriptor: Kinesin-like protein Klp61F (1 entity in total)
• Functional Keywords: kinesin-5, bipolar assembly, four-helical-bundle, cell cycle
• Biological source: Drosophila melanogaster (Fruit fly)
• Total number of polymer chains: 4
• Total formula weight: 113732.88

Authors

Nithianantham, S.,Al-Bassam, J. (deposition date: 2021-09-12, release date: 2023-03-15, Last modification date: 2023-10-25)

Primary citation

Nithianantham, S.,Iwanski, M.K.,Gaska, I.,Pandey, H.,Bodrug, T.,Inagaki, S.,Major, J.,Brouhard, G.J.,Gheber, L.,Rosenfeld, S.S.,Forth, S.,Hendricks, A.G.,Al-Bassam, J.
The kinesin-5 tail and bipolar miniflament domains are the origin of its microtubule crosslinking and sliding activity.
Mol.Biol.Cell, :mbcE23070287-mbcE23070287, 2023

PubMed Abstract: Kinesin-5 crosslinks and slides apart microtubules to assemble, elongate, and maintain the mitotic spindle. Kinesin-5 is a tetramer, where two N-terminal motor domains are positioned at each end of the motor, and the coiled-coil stalk domains are organized into a tetrameric bundle through the bipolar assembly (BASS) domain. To dissect the function of the individual structural elements of the motor, we constructed a minimal kinesin-5 tetramer (mini-tetramer). We determined the x-ray structure of the extended, 34-nm BASS domain. Guided by these structural studies, we generated active bipolar kinesin-5 mini-tetramer motors from and human orthologues which are half the length of native kinesin-5. We then used these kinesin-5 mini-tetramers to examine the role of two unique structural adaptations of kinesin-5: 1) the length and flexibility of the tetramer, and 2) the C-terminal tails which interact with the motor domains to coordinate their ATPase activity. The C-terminal domain causes frequent pausing and clustering of kinesin-5. By comparing microtubule crosslinking and sliding by mini-tetramer and full-length kinesin-5, we find that both the length and flexibility of kinesin-5 and the C-terminal tails govern its ability to crosslink microtubules. Once crosslinked, stiffer mini-tetramers slide antiparallel microtubules more efficiently than full-length motors.

PubMed: 37610838
DOI: 10.1091/mbc.E23-07-0287

Experimental method

X-RAY DIFFRACTION (4.41 Å)