Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6RLA

Structure of the dynein-2 complex; motor domains

Summary for 6RLA
Entry DOI10.2210/pdb6rla/pdb
EMDB information4917
DescriptorO6-alkylguanine-DNA alkyltransferase mutant,DYNC2H1 variant protein, ADENOSINE-5'-DIPHOSPHATE, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
Functional Keywordsdynein, cilia, intraflagellar transport, complex, motor protein
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains2
Total formula weight1034072.24
Authors
Toropova, K.,Zalyte, R.,Mukhopadhyay, A.G.,Mladenov, M.,Carter, A.P.,Roberts, A.J. (deposition date: 2019-05-01, release date: 2019-08-28, Last modification date: 2024-05-22)
Primary citationToropova, K.,Zalyte, R.,Mukhopadhyay, A.G.,Mladenov, M.,Carter, A.P.,Roberts, A.J.
Structure of the dynein-2 complex and its assembly with intraflagellar transport trains.
Nat.Struct.Mol.Biol., 26:823-829, 2019
Cited by
PubMed Abstract: Dynein-2 assembles with polymeric intraflagellar transport (IFT) trains to form a transport machinery that is crucial for cilia biogenesis and signaling. Here we recombinantly expressed the ~1.4-MDa human dynein-2 complex and solved its cryo-EM structure to near-atomic resolution. The two identical copies of the dynein-2 heavy chain are contorted into different conformations by a WDR60-WDR34 heterodimer and a block of two RB and six LC8 light chains. One heavy chain is steered into a zig-zag conformation, which matches the periodicity of the anterograde IFT-B train. Contacts between adjacent dyneins along the train indicate a cooperative mode of assembly. Removal of the WDR60-WDR34-light chain subcomplex renders dynein-2 monomeric and relieves autoinhibition of its motility. Our results converge on a model in which an unusual stoichiometry of non-motor subunits controls dynein-2 assembly, asymmetry, and activity, giving mechanistic insight into the interaction of dynein-2 with IFT trains and the origin of diverse functions in the dynein family.
PubMed: 31451806
DOI: 10.1038/s41594-019-0286-y
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.9 Å)
Structure validation

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon