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	Microtubule association induces a Mg-free apo-like ADP pre-release conformation in kinesin-1 that is unaffected by its autoinhibitory tail.
Journal, issue, pages	Nat Commun, Vol. 16, Issue 1, Page 6214, Year 2025
Publish date	Jul 5, 2025
Authors	J Atherton / M S Chegkazi / M Leusciatti / M Di Palma / E Peirano / L S Pozzer / M V A Meli / S Pasqualato / T Foran / G Morra / R A Steiner /
PubMed Abstract	Kinesin-1 is a processive dimeric ATP-driven motor that transports vital intracellular cargos along microtubules (MTs). If not engaged in active transport, kinesin-1 limits futile ATP hydrolysis by ...Kinesin-1 is a processive dimeric ATP-driven motor that transports vital intracellular cargos along microtubules (MTs). If not engaged in active transport, kinesin-1 limits futile ATP hydrolysis by adopting a compact autoinhibited conformation that involves an interaction between its C-terminal tail and the N-terminal motor domains. Here, using a chimeric kinesin-1 that fuses the N-terminal motor region to the tail and a tail variant unable to interact with the motors, we employ cryo-EM to investigate elements of the MT-associated mechanochemical cycle. We describe a missing structure for the proposed two-step allosteric mechanism of ADP release, the ATPase rate limiting step. It shows that MT association remodels the hydrogen bond network at the nucleotide binding site triggering removal of the Mg ion from the Mg-ADP complex. This results in a strong MT-binding apo-like state before ADP dissociation, which molecular dynamics simulations indicate is mediated by loop 9 dynamics. We further demonstrate that tail association does not directly affect this mechanism, nor the adoption of the ATP hydrolysis-competent conformation, nor neck linker docking/undocking, even when zippering the two motor domains. We propose a revised mechanism for tail-dependent kinesin-1 autoinhibition and suggest a possible explanation for its characteristic pausing behavior on MTs.
External links	Nat Commun / PubMed:40617823 / PubMed Central
Methods	EM (single particle)
Resolution	2.9 - 3.6 Å
Structure data	19174 8rhb EMDB-19174, PDB-8rhb: Microtubule-associated kinesin-1 tail complex bound to AMPPNP, single-headed state Method: EM (single particle) / Resolution: 3.0 Å 19176 8rhh EMDB-19176, PDB-8rhh: Microtubule-associated kinesin-1 tail complex bound to AMPPNP, two-headed state Method: EM (single particle) / Resolution: 3.0 Å 19188 8rik EMDB-19188, PDB-8rik: Microtubule-associated kinesin-1 tail complex bound to ADP, single-headed state Method: EM (single particle) / Resolution: 3.6 Å 19192 8riz EMDB-19192, PDB-8riz: Microtubule-associated kinesin-1 tail complex bound to ADP, two-headed state Method: EM (single particle) / Resolution: 3.6 Å 51477 9gnq EMDB-51477, PDB-9gnq: Microtubule-associated Kif5B IAK tail mutant bound to ADP Method: EM (single particle) / Resolution: 2.9 Å
Chemicals	ChemComp-GDP: GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying moleculeYM ChemComp-TA1: TAXOL / medication, chemotherapyYM ChemComp-ANP: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogueYM ChemComp-MG: Unknown entry ChemComp-GTP: GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying moleculeYM ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM
Source	homo sapiens (human) sus scrofa (pig)
Keywords	MOTOR PROTEIN / Kinesin autoinhibition motor microtubules mechanochemistry intracellular transport / Kinesin / microtubules / tail / autoihibition / IAK / transport