5AYH

Structure of the entire dynein stalk region

Summary for 5AYH

• Entry DOI: 10.2210/pdb5ayh/pdb
• Related: 3WUQ
• Descriptor: Cytoplasmic dynein 1 heavy chain 1 (1 entity in total)
• Functional Keywords: microtubule, motor protein
• Biological source: Mus musculus (Mouse)
• Total number of polymer chains: 1
• Total formula weight: 31716.35

Authors

Kurisu, G.,Nishikawa, Y.,Inatomi, M. (deposition date: 2015-08-21, release date: 2015-12-16, Last modification date: 2025-03-12)

Primary citation

Nishikawa, Y.,Inatomi, M.,Iwasaki, H.,Kurisu, G.
Structural Change in the Dynein Stalk Region Associated with Two Different Affinities for the Microtubule
J.Mol.Biol., 428:1886-1896, 2016

PubMed Abstract: Dynein is a large microtubule-based motor complex that requires tight coupling of intra-molecular ATP hydrolysis with the generation of mechanical force and track-binding activity. However, the microtubule-binding domain is structurally separated by about 15nm from the nucleotide-binding sites by a coiled-coil stalk. Thus, long-range two-way communication is necessary for coordination between the catalytic cycle of ATP hydrolysis and dynein's track-binding affinities. To investigate the structural changes that occur in the dynein stalk region to produce two different microtubule affinities, here we improve the resolution limit of the previously reported structure of the entire stalk region and we investigate structural changes in the dynein stalk and strut/buttress regions by comparing currently available X-ray structures. In the light of recent crystal structures, the basis of the transition from the low-affinity to the high-affinity coiled-coil registry is discussed. A concerted movement model previously reported by Carter and Vale is modified more specifically, and we proposed it as the open zipper model.

PubMed: 26585405
DOI: 10.1016/j.jmb.2015.11.008

Experimental method

X-RAY DIFFRACTION (3.011 Å)