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	Comprehensive structural model of the mechanochemical cycle of a mitotic motor highlights molecular adaptations in the kinesin family.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 111, Issue 5, Page 1837-1842, Year 2014
Publish date	Feb 4, 2014
Authors	Adeline Goulet / Jennifer Major / Yonggun Jun / Steven P Gross / Steven S Rosenfeld / Carolyn A Moores /
PubMed Abstract	Kinesins are responsible for a wide variety of microtubule-based, ATP-dependent functions. Their motor domain drives these activities, but the molecular adaptations that specify these diverse and ...Kinesins are responsible for a wide variety of microtubule-based, ATP-dependent functions. Their motor domain drives these activities, but the molecular adaptations that specify these diverse and essential cellular activities are poorly understood. It has been assumed that the first identified kinesin--the transport motor kinesin-1--is the mechanistic paradigm for the entire superfamily, but accumulating evidence suggests otherwise. To address the deficits in our understanding of the molecular basis of functional divergence within the kinesin superfamily, we studied kinesin-5s, which are essential mitotic motors whose inhibition blocks cell division. Using cryo-electron microscopy and determination of structure at subnanometer resolution, we have visualized conformations of microtubule-bound human kinesin-5 motor domain at successive steps in its ATPase cycle. After ATP hydrolysis, nucleotide-dependent conformational changes in the active site are allosterically propagated into rotations of the motor domain and uncurling of the drug-binding loop L5. In addition, the mechanical neck-linker element that is crucial for motor stepping undergoes discrete, ordered displacements. We also observed large reorientations of the motor N terminus that indicate its importance for kinesin-5 function through control of neck-linker conformation. A kinesin-5 mutant lacking this N terminus is enzymatically active, and ATP-dependent neck-linker movement and motility are defective, although not ablated. All these aspects of kinesin-5 mechanochemistry are distinct from kinesin-1. Our findings directly demonstrate the regulatory role of the kinesin-5 N terminus in collaboration with the motor's structured neck-linker and highlight the multiple adaptations within kinesin motor domains that tune their mechanochemistries according to distinct functional requirements.
External links	Proc Natl Acad Sci U S A / PubMed:24449904 / PubMed Central
Methods	EM (single particle)
Resolution	9.2 - 25.0 Å
Structure data	2533 4ck6 4ck7 EMDB-2533: Electron cryo-microscopy of microtubule-bound human kinesin-5 motor domain in the ADP.AlFx state. PDB-4ck6: Pseudo-atomic model of microtubule-bound human kinesin-5 motor domain in the ADP.AlFx state, based on cryo-electron microscopy experiment. PDB-4ck7: Pseudo-atomic model of microtubule-bound human kinesin-5 motor domain in presence of adp.alfx (NECK-LINKER IN ITS DISCONNECTED CONFORMATION, based on cryo-electron microscopy experiment Method: EM (single particle) / Resolution: 9.2 Å EMDB-2534: Cryo-electron microscopy of microtubule-bound human kinesin-5 motor domain in the ADP.AlFx state (gold cluster in the loop5 T126C). Method: EM (single particle) / Resolution: 19.0 Å EMDB-2535: cryo-electron microscopy of microtubule-bound human kinesin-5 motor domain in the ADP.AlFx state (gold cluster in the neck linker V365C). Method: EM (single particle) / Resolution: 16.0 Å EMDB-2536: cryo-electron microscopy of microtubule-bound human kinesin-5 motor domain in the ADP.AlFx state (gold cluster in the N-terminus A9C). Method: EM (single particle) / Resolution: 18.0 Å 2537 4ck5 EMDB-2537: cryo-electron microscopy of microtubule-bound human kinesin-5 motor domain in the ADP state PDB-4ck5: Pseudo-atomic model of microtubule-bound human kinesin-5 motor domain in the ADP state, based on cryo-electron microscopy experiment. Method: EM (single particle) / Resolution: 10.0 Å EMDB-2538: cryo-electron microscopy of microtubule-bound human kinesin-5 motor domain in the ADP state with a gold cluster attached to the loop5 (T126C) Method: EM (single particle) / Resolution: 18.0 Å EMDB-2539: cryo-electron microscopy of microtubule-bound human kinesin-5 motor domain in the ADP state (gold cluster in the neck linker V365C). Method: EM (single particle) / Resolution: 20.0 Å EMDB-2540: cryo-electron microscopy of microtubule-bound human kinesin-5 motor domain in the ADP state (gold cluster in the N-terminus A9C). Method: EM (single particle) / Resolution: 18.0 Å EMDB-2541: cryo-electron microscopy of microtubule-bound human kinesin-5 motor domain in the AMPPNP state (gold cluster in the N-terminus A9C). Method: EM (single particle) / Resolution: 25.0 Å EMDB-2542: cryo-electron microscopy of microtubule-bound human kinesin-5 motor domain in rigor (gold cluster in the N-terminus A9C). Method: EM (single particle) / Resolution: 18.0 Å
Chemicals	ChemComp-GTP: GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying moleculeYM / Guanosine triphosphate ChemComp-GDP: GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying moleculeYM / Guanosine diphosphate ChemComp-TA1: TAXOL / medication, chemotherapyYM / Paclitaxel ChemComp-MG: Unknown entry ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM / Adenosine diphosphate ChemComp-AF3: ALUMINUM FLUORIDE / Aluminium fluoride
Source	bos taurus (cattle) homo sapiens (human)
Keywords	MOTOR PROTEIN / KINESINS / MICROTUBULES / MITOSIS / MECHANOCHEMISTRY