3J6P

Pseudo-atomic model of dynein microtubule binding domain-tubulin complex based on a cryoEM map

Summary for 3J6P

• Entry DOI: 10.2210/pdb3j6p/pdb
• EMDB information: 5931
• Descriptor: Dynein heavy chain, cytoplasmic, Tubulin alpha-1A chain, Tubulin beta chain, ... (7 entities in total)
• Functional Keywords: motor protein-cytoskeleton complex, motor protein-structural protein complex, motor protein/structural protein
• Biological source: Dictyostelium discoideum (Slime mold); More
• Cellular location: Cytoplasm, cytoskeleton: P34036 P02550 P02554
• Total number of polymer chains: 3
• Total formula weight: 114187.16

Authors

Uchimura, S.,Fujii, T.,Takazaki, H.,Ayukawa, R.,Nishikawa, Y.,Minoura, I.,Hachikubo, Y.,Kurisu, G.,Sutoh, K.,Kon, T.,Namba, K.,Muto, E. (deposition date: 2014-03-20, release date: 2014-12-31, Last modification date: 2024-03-20)

Primary citation

Uchimura, S.,Fujii, T.,Takazaki, H.,Ayukawa, R.,Nishikawa, Y.,Minoura, I.,Hachikubo, Y.,Kurisu, G.,Sutoh, K.,Kon, T.,Namba, K.,Muto, E.
A flipped ion pair at the dynein-microtubule interface is critical for dynein motility and ATPase activation
J.Cell Biol., 208:211-222, 2015

PubMed Abstract: Dynein is a motor protein that moves on microtubules (MTs) using the energy of adenosine triphosphate (ATP) hydrolysis. To understand its motility mechanism, it is crucial to know how the signal of MT binding is transmitted to the ATPase domain to enhance ATP hydrolysis. However, the molecular basis of signal transmission at the dynein-MT interface remains unclear. Scanning mutagenesis of tubulin identified two residues in α-tubulin, R403 and E416, that are critical for ATPase activation and directional movement of dynein. Electron cryomicroscopy and biochemical analyses revealed that these residues form salt bridges with the residues in the dynein MT-binding domain (MTBD) that work in concert to induce registry change in the stalk coiled coil and activate the ATPase. The R403-E3390 salt bridge functions as a switch for this mechanism because of its reversed charge relative to other residues at the interface. This study unveils the structural basis for coupling between MT binding and ATPase activation and implicates the MTBD in the control of directional movement.

PubMed: 25583999
DOI: 10.1083/jcb.201407039

Experimental method

ELECTRON MICROSCOPY (8.2 Å)