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Structure paper

TitleCryo-EM Reveals How Human Cytoplasmic Dynein Is Auto-inhibited and Activated.
Journal, issue, pagesCell, Vol. 169, Issue 7, Page 1303-1314.e18, Year 2017
Publish dateJun 15, 2017
AuthorsKai Zhang / Helen E Foster / Arnaud Rondelet / Samuel E Lacey / Nadia Bahi-Buisson / Alexander W Bird / Andrew P Carter /
PubMed AbstractCytoplasmic dynein-1 binds dynactin and cargo adaptor proteins to form a transport machine capable of long-distance processive movement along microtubules. However, it is unclear why dynein-1 moves ...Cytoplasmic dynein-1 binds dynactin and cargo adaptor proteins to form a transport machine capable of long-distance processive movement along microtubules. However, it is unclear why dynein-1 moves poorly on its own or how it is activated by dynactin. Here, we present a cryoelectron microscopy structure of the complete 1.4-megadalton human dynein-1 complex in an inhibited state known as the phi-particle. We reveal the 3D structure of the cargo binding dynein tail and show how self-dimerization of the motor domains locks them in a conformation with low microtubule affinity. Disrupting motor dimerization with structure-based mutagenesis drives dynein-1 into an open form with higher affinity for both microtubules and dynactin. We find the open form is also inhibited for movement and that dynactin relieves this by reorienting the motor domains to interact correctly with microtubules. Our model explains how dynactin binding to the dynein-1 tail directly stimulates its motor activity.
External linksCell / PubMed:28602352 / PubMed Central
MethodsEM (single particle)
Resolution3.8 - 15.0 Å
Structure data

3698

5nug

EMDB-3698, PDB-5nug:
Motor domains from human cytoplasmic dynein-1 in the phi-particle conformation
Method: EM (single particle) / Resolution: 3.8 Å

3703

5nvs

EMDB-3703, PDB-5nvs:
Human cytoplasmic dynein-1 tail in the twisted N-terminus state
Method: EM (single particle) / Resolution: 8.4 Å

EMDB-3704:
Human cytoplasmic dynein-1 tail in the parallel state
Method: EM (single particle) / Resolution: 12.0 Å

3705

5nvu

EMDB-3705, PDB-5nvu:
Full length human cytoplasmic dynein-1 in the phi-particle conformation
Method: EM (single particle) / Resolution: 15.0 Å

3706

5nw4

EMDB-3706, PDB-5nw4:
Human cytoplasmic dynein-1 bound to dynactin and an N-terminal construct of BICD2
Method: EM (single particle) / Resolution: 8.7 Å

EMDB-3707:
Locally refined human cytoplasmic dynein-1 tail bound to dynactin and an N-terminal construct of BICD2
Method: EM (single particle) / Resolution: 12.0 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
  • sus scrofa (pig)
  • Pig (pig)
KeywordsMOTOR PROTEIN / dynein / motor domain / AAA+ / tail complex / dynein-1 / phi-particle / dynactin / BICD

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