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Structure paper

TitleConserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins.
Journal, issue, pagesElife, Vol. 3, Page e03680, Year 2014
Publish dateSep 10, 2014
AuthorsJoseph Atherton / Irene Farabella / I-Mei Yu / Steven S Rosenfeld / Anne Houdusse / Maya Topf / Carolyn A Moores /
PubMed AbstractKinesins are a superfamily of microtubule-based ATP-powered motors, important for multiple, essential cellular functions. How microtubule binding stimulates their ATPase and controls force generation ...Kinesins are a superfamily of microtubule-based ATP-powered motors, important for multiple, essential cellular functions. How microtubule binding stimulates their ATPase and controls force generation is not understood. To address this fundamental question, we visualized microtubule-bound kinesin-1 and kinesin-3 motor domains at multiple steps in their ATPase cycles--including their nucleotide-free states--at ∼ 7 Å resolution using cryo-electron microscopy. In both motors, microtubule binding promotes ordered conformations of conserved loops that stimulate ADP release, enhance microtubule affinity and prime the catalytic site for ATP binding. ATP binding causes only small shifts of these nucleotide-coordinating loops but induces large conformational changes elsewhere that allow force generation and neck linker docking towards the microtubule plus end. Family-specific differences across the kinesin-microtubule interface account for the distinctive properties of each motor. Our data thus provide evidence for a conserved ATP-driven mechanism for kinesins and reveal the critical mechanistic contribution of the microtubule interface.
External linksElife / PubMed:25209998 / PubMed Central
MethodsEM (single particle)
Resolution6.3 - 7.7 Å
Structure data

2765

4uxo

EMDB-2765, PDB-4uxo:
Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins
Method: EM (single particle) / Resolution: 6.3 Å

2766

4uxp

EMDB-2766, PDB-4uxp:
Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins
Method: EM (single particle) / Resolution: 7.0 Å

2767

4uxr

EMDB-2767, PDB-4uxr:
Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins
Method: EM (single particle) / Resolution: 7.0 Å

2768

4uxs

EMDB-2768, PDB-4uxs:
Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins
Method: EM (single particle) / Resolution: 7.0 Å

2769

4uxt

EMDB-2769, PDB-4uxt:
Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins
Method: EM (single particle) / Resolution: 7.4 Å

2770

4uxy

EMDB-2770, PDB-4uxy:
Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins
Method: EM (single particle) / Resolution: 6.5 Å

2771

4uy0

EMDB-2771, PDB-4uy0:
Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins
Method: EM (single particle) / Resolution: 7.7 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM

ChemComp-TA1:
TAXOL / medication, chemotherapy*YM

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

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

ChemComp-ALF:
TETRAFLUOROALUMINATE ION

Source
  • bos taurus (cattle)
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / KINESIN / MICROTUBULE / CRYO-EM

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