6KJN

The microtubule-binding domains of yeast cytoplasmic dynein in the high affinity state

Summary for 6KJN

• Entry DOI: 10.2210/pdb6kjn/pdb
• Descriptor: Dynein heavy chain, cytoplasmic (1 entity in total)
• Functional Keywords: microtubule, dynein, disulfide bond, high affinity, motor protein
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 16499.87

Authors

Nishida, N.,Komori, Y.,Takarada, O.,Watanabe, A.,Tamura, S.,Kubo, S.,Shimada, I.,Kikkawa, M. (deposition date: 2019-07-22, release date: 2020-03-18, Last modification date: 2024-10-16)

Primary citation

Nishida, N.,Komori, Y.,Takarada, O.,Watanabe, A.,Tamura, S.,Kubo, S.,Shimada, I.,Kikkawa, M.
Structural basis for two-way communication between dynein and microtubules.
Nat Commun, 11:1038-1038, 2020

PubMed Abstract: The movements of cytoplasmic dynein on microtubule (MT) tracks is achieved by two-way communication between the microtubule-binding domain (MTBD) and the ATPase domain via a coiled-coil stalk, but the structural basis of this communication remains elusive. Here, we regulate MTBD either in high-affinity or low-affinity states by introducing a disulfide bond to the stalk and analyze the resulting structures by NMR and cryo-EM. In the MT-unbound state, the affinity changes of MTBD are achieved by sliding of the stalk α-helix by a half-turn, which suggests that structural changes propagate from the ATPase-domain to MTBD. In addition, MT binding induces further sliding of the stalk α-helix even without the disulfide bond, suggesting how the MT-induced conformational changes propagate toward the ATPase domain. Based on differences in the MT-binding surface between the high- and low-affinity states, we propose a potential mechanism for the directional bias of dynein movement on MT tracks.

PubMed: 32098965
DOI: 10.1038/s41467-020-14842-8

Experimental method

SOLUTION NMR