Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Cryo-EM shows how dynactin recruits two dyneins for faster movement.
Journal, issue, pages	Nature, Vol. 554, Issue 7691, Page 202-206, Year 2018
Publish date	Feb 7, 2018
Authors	Linas Urnavicius / Clinton K Lau / Mohamed M Elshenawy / Edgar Morales-Rios / Carina Motz / Ahmet Yildiz / Andrew P Carter /
PubMed Abstract	Dynein and its cofactor dynactin form a highly processive microtubule motor in the presence of an activating adaptor, such as BICD2. Different adaptors link dynein and dynactin to distinct cargoes. ...Dynein and its cofactor dynactin form a highly processive microtubule motor in the presence of an activating adaptor, such as BICD2. Different adaptors link dynein and dynactin to distinct cargoes. Here we use electron microscopy and single-molecule studies to show that adaptors can recruit a second dynein to dynactin. Whereas BICD2 is biased towards recruiting a single dynein, the adaptors BICDR1 and HOOK3 predominantly recruit two dyneins. We find that the shift towards a double dynein complex increases both the force and speed of the microtubule motor. Our 3.5 Å resolution cryo-electron microscopy reconstruction of a dynein tail-dynactin-BICDR1 complex reveals how dynactin can act as a scaffold to coordinate two dyneins side-by-side. Our work provides a structural basis for understanding how diverse adaptors recruit different numbers of dyneins and regulate the motile properties of the dynein-dynactin transport machine.
External links	Nature / PubMed:29420470 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	1.79 - 8.2 Å
Structure data	4168 6f1t EMDB-4168, PDB-6f1t: Cryo-EM structure of two dynein tail domains bound to dynactin and BICDR1 Method: EM (single particle) / Resolution: 3.5 Å 4169 6f1u EMDB-4169, PDB-6f1u: N terminal region of dynein tail domains in complex with dynactin filament and BICDR-1 Method: EM (single particle) / Resolution: 3.4 Å 4170 6f1v EMDB-4170, PDB-6f1v: C terminal region of the dynein heavy chains in the dynein tail/dynactin/BICDR1 complex Method: EM (single particle) / Resolution: 3.4 Å 4171 6f1y EMDB-4171, PDB-6f1y: Dynein light intermediate chain region of the dynein tail/dynactin/BICDR1 complex Method: EM (single particle) / Resolution: 3.4 Å 4172 6f1z EMDB-4172, PDB-6f1z: Roadblock-1 region of the dynein tail/dynactin/BICDR1 complex Method: EM (single particle) / Resolution: 3.4 Å 4177 6f38 EMDB-4177, PDB-6f38: Cryo-EM structure of two dynein tail domains bound to dynactin and HOOK3 Method: EM (single particle) / Resolution: 6.7 Å PDB-5owo: Human cytoplasmic Dynein N-Terminus dimerization domain at 1.8 Angstrom resolution Method: X-RAY DIFFRACTION / Resolution: 1.79 Å PDB-6f3a: Cryo-EM structure of a single dynein tail domain bound to dynactin and BICD2N Method: ELECTRON MICROSCOPY / Resolution: 8.2 Å
Chemicals	ChemComp-GOL: GLYCEROL / Glycerol ChemComp-MG: Unknown entry ChemComp-CA: Unknown entry ChemComp-NA: Unknown entry ChemComp-K: Unknown entry ChemComp-HOH: WATER / Water ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM / Adenosine diphosphate ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM / Adenosine triphosphate
Source	mus musculus (house mouse) homo sapiens (human) sus scrofa (pig) Pig (pig)
Keywords	MOTOR PROTEIN / Dynein / Heavy chain / Dimerization domain / Cryo-EM / Complex / dynein/dynactin/BICDR / TDR / Cargo adaptor / TDH / DDH / dynein/dynactin/HOOK3 / TDB / dynein/dynactin/BICD2