3ERR

Microtubule binding domain from mouse cytoplasmic dynein as a fusion with seryl-tRNA synthetase

Summary for 3ERR

• Entry DOI: 10.2210/pdb3err/pdb
• Descriptor: fusion protein of microtubule binding domain from mouse cytoplasmic dynein and seryl-tRNA synthetase from Thermus thermophilus, ADENOSINE MONOPHOSPHATE (3 entities in total)
• Functional Keywords: dynein, microtubule binding domain, coiled coil, fusion protein, ligase
• Biological source: Mus musculus; More
• Cellular location: Cytoplasm : P34945
• Total number of polymer chains: 2
• Total formula weight: 122609.91

Authors

Carter, A.P. (deposition date: 2008-10-03, release date: 2008-11-25, Last modification date: 2023-09-06)

Primary citation

Carter, A.P.,Garbarino, J.E.,Wilson-Kubalek, E.M.,Shipley, W.E.,Cho, C.,Milligan, R.A.,Vale, R.D.,Gibbons, I.R.
Structure and functional role of dynein's microtubule-binding domain.
Science, 322:1691-1695, 2008

PubMed Abstract: Dynein motors move various cargos along microtubules within the cytoplasm and power the beating of cilia and flagella. An unusual feature of dynein is that its microtubule-binding domain (MTBD) is separated from its ring-shaped AAA+ adenosine triphosphatase (ATPase) domain by a 15-nanometer coiled-coil stalk. We report the crystal structure of the mouse cytoplasmic dynein MTBD and a portion of the coiled coil, which supports a mechanism by which the ATPase domain and MTBD may communicate through a shift in the heptad registry of the coiled coil. Surprisingly, functional data suggest that the MTBD, and not the ATPase domain, is the main determinant of the direction of dynein motility.

PubMed: 19074350
DOI: 10.1126/science.1164424

Experimental method

X-RAY DIFFRACTION (2.27 Å)