PDBsum entry 6f1v

Motor protein

PDB id: 6f1v

Contents

Protein chains

411 a.a.

217 a.a.

PDB id:

6f1v

Name:

Motor protein

Title:

C terminal region of the dynein heavy chains in the dynein tail/dynactin/bicdr1 complex

Structure:

Cytoplasmic dynein 1 heavy chain 1. Chain: f, m. Synonym: cytoplasmic dynein heavy chain 1,dynein heavy chain, cytosolic. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: dync1h1, dhc1, dnch1, dncl, dnecl, dyhc, kiaa0325. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108

Authors:

L.Urnavicius,C.K.Lau,M.M.Elshenawy,E.Morales-Rios,C.Motz,A.Yildiz, A.P.Carter

Key ref:

L.Urnavicius et al. (2018). Cryo-EM shows how dynactin recruits two dyneins for faster movement. Nature, 554, 202-206. PubMed id: 29420470 DOI: 10.1038/nature25462

Date:

23-Nov-17 Release date: 17-Jan-18

Protein chain

Q14204  (DYHC1_HUMAN) -  Cytoplasmic dynein 1 heavy chain 1 from Homo sapiens

Seq: 4646 a.a.

Struc: 411 a.a.

Protein chain

Q14204  (DYHC1_HUMAN) -  Cytoplasmic dynein 1 heavy chain 1 from Homo sapiens

Seq: 4646 a.a.

Struc: 217 a.a.

Enzyme reactions

• Enzyme class: Chains f, m: E.C.?

DOI no: 10.1038/nature25462

Nature 554:202-206 (2018)

PubMed id: 29420470

Cryo-EM shows how dynactin recruits two dyneins for faster movement.

L.Urnavicius, C.K.Lau, M.M.Elshenawy, E.Morales-Rios, C.Motz, A.Yildiz, A.P.Carter.

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. 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.