4W8F

Crystal structure of the dynein motor domain in the AMPPNP-bound state

Summary for 4W8F

• Entry DOI: 10.2210/pdb4w8f/pdb
• Descriptor: Dynein heavy chain lysozyme chimera, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION (3 entities in total)
• Functional Keywords: cytoplasmic dynein, microtubule, atpase, aaa+, amppnp, motor protein
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Total number of polymer chains: 2
• Total formula weight: 613877.93

Authors

Cheng, H.-C.,Bhabha, G.,Zhang, N.,Vale, R.D. (deposition date: 2014-08-24, release date: 2014-11-12, Last modification date: 2023-12-27)

Primary citation

Bhabha, G.,Cheng, H.C.,Zhang, N.,Moeller, A.,Liao, M.,Speir, J.A.,Cheng, Y.,Vale, R.D.
Allosteric communication in the Dynein motor domain.
Cell, 159:857-868, 2014

PubMed Abstract: Dyneins power microtubule motility using ring-shaped, AAA-containing motor domains. Here, we report X-ray and electron microscopy (EM) structures of yeast dynein bound to different ATP analogs, which collectively provide insight into the roles of dynein's two major ATPase sites, AAA1 and AAA3, in the conformational change mechanism. ATP binding to AAA1 triggers a cascade of conformational changes that propagate to all six AAA domains and cause a large movement of the "linker," dynein's mechanical element. In contrast to the role of AAA1 in driving motility, nucleotide transitions in AAA3 gate the transmission of conformational changes between AAA1 and the linker, suggesting that AAA3 acts as a regulatory switch. Further structural and mutational studies also uncover a role for the linker in regulating the catalytic cycle of AAA1. Together, these results reveal how dynein's two major ATP-binding sites initiate and modulate conformational changes in the motor domain during motility.

PubMed: 25417161
DOI: 10.1016/j.cell.2014.10.018

Experimental method

X-RAY DIFFRACTION (3.541 Å)