8I3J

Crystal structure of human inner-arm dynein heavy chain d stalk and microtubule binding domain

Summary for 8I3J

• Entry DOI: 10.2210/pdb8i3j/pdb
• Descriptor: Dynein axonemal heavy chain 1 (1 entity in total)
• Functional Keywords: contractile protein, motor protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 31487.84

Authors

Ko, S.,Yu, J.,Toda, A.,Tanaka, H.,Kurisu, G. (deposition date: 2023-01-17, release date: 2023-08-09, Last modification date: 2024-10-09)

Primary citation

Ko, S.,Toda, A.,Tanaka, H.,Yu, J.,Kurisu, G.
Crystal structure of the stalk region of axonemal inner-arm dynein-d reveals unique features in the coiled-coil and microtubule-binding domain.
Febs Lett., 597:2149-2160, 2023

PubMed Abstract: Axonemal dynein is an ATP-dependent microtubular motor protein responsible for cilia and flagella beating, and its dysfunction can cause diseases such as primary ciliary dyskinesia and sperm dysmotility. Despite its biological importance, structure-based mechanisms underlying axonemal dynein motors remain unclear. Here, we determined the X-ray crystal structure of the human inner-arm dynein-d (DNAH1) stalk region, which contains a long antiparallel coiled-coil and a microtubule-binding domain (MTBD), at 2.7 Å resolution. Notably, differences in the relative orientation of the coiled-coil and MTBD in comparison with other dyneins, as well as the diverse orientations of the MTBD flap region among various isoforms, lead us to propose a 'spike shoe model' with an altered stepping angle for the interaction between IAD-d and microtubules. Based on these findings, we discuss isoform-specific functions of the axonemal dynein stalk MTBDs.

PubMed: 37400274
DOI: 10.1002/1873-3468.14690

Experimental method

X-RAY DIFFRACTION (2.69 Å)