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	Structural basis of mechano-chemical coupling by the mitotic kinesin KIF14.
Journal, issue, pages	Nat Commun, Vol. 12, Issue 1, Page 3637, Year 2021
Publish date	Jun 15, 2021
Authors	Matthieu P M H Benoit / Ana B Asenjo / Mohammadjavad Paydar / Sabin Dhakal / Benjamin H Kwok / Hernando Sosa /
PubMed Abstract	KIF14 is a mitotic kinesin whose malfunction is associated with cerebral and renal developmental defects and several cancers. Like other kinesins, KIF14 couples ATP hydrolysis and microtubule binding ...KIF14 is a mitotic kinesin whose malfunction is associated with cerebral and renal developmental defects and several cancers. Like other kinesins, KIF14 couples ATP hydrolysis and microtubule binding to the generation of mechanical work, but the coupling mechanism between these processes is still not fully clear. Here we report 20 high-resolution (2.7-3.9 Å) cryo-electron microscopy KIF14-microtubule structures with complementary functional assays. Analysis procedures were implemented to separate coexisting conformations of microtubule-bound monomeric and dimeric KIF14 constructs. The data provide a comprehensive view of the microtubule and nucleotide induced KIF14 conformational changes. It shows that: 1) microtubule binding, the nucleotide species, and the neck-linker domain govern the transition between three major conformations of the motor domain; 2) an undocked neck-linker prevents the nucleotide-binding pocket to fully close and dampens ATP hydrolysis; 3) 13 neck-linker residues are required to assume a stable docked conformation; 4) the neck-linker position controls the hydrolysis rather than the nucleotide binding step; 5) the two motor domains of KIF14 dimers adopt distinct conformations when bound to the microtubule; and 6) the formation of the two-heads-bound-state introduces structural changes in both motor domains of KIF14 dimers. These observations provide the structural basis for a coordinated chemo-mechanical kinesin translocation model.
External links	Nat Commun / PubMed:34131133 / PubMed Central
Methods	EM (helical sym.)
Resolution	2.7 - 3.9 Å
Structure data	21932 6wwe EMDB-21932, PDB-6wwe: Apo KIF14[391-772] in complex with a microtubule Method: EM (helical sym.) / Resolution: 3.9 Å 21933 6wwf EMDB-21933, PDB-6wwf: KIF14[391-772] - ADP in complex with a microtubule Method: EM (helical sym.) / Resolution: 3.3 Å 21934 6wwg EMDB-21934, PDB-6wwg: KIF14[391-772] dimer two-heads-bound state - ADP-AlFx in complex with a microtubule Method: EM (helical sym.) / Resolution: 2.9 Å 21935 6wwh EMDB-21935, PDB-6wwh: KIF14[391-772] dimer two-heads-bound state - AMP-PNP in complex with a microtubule Method: EM (helical sym.) / Resolution: 3.8 Å 21936 6wwi EMDB-21936, PDB-6wwi: Apo KIF14[391-755] in complex with a microtubule Method: EM (helical sym.) / Resolution: 3.6 Å 21937 6wwj EMDB-21937, PDB-6wwj: KIF14[391-755] - ADP in complex with a microtubule Method: EM (helical sym.) / Resolution: 3.4 Å 21938 6wwk EMDB-21938, PDB-6wwk: KIF14[391-755] dimer two-heads-bound state - ADP-AlFx in complex with a microtubule Method: EM (helical sym.) / Resolution: 3.0 Å 21939 6wwl EMDB-21939, PDB-6wwl: KIF14[391-755] dimer two-heads-bound state - AMP-PNP in complex with a microtubule Method: EM (helical sym.) / Resolution: 3.1 Å 21940 6wwm EMDB-21940, PDB-6wwm: KIF14[391-748] - ADP in complex with a microtubule Method: EM (helical sym.) / Resolution: 2.8 Å 21941 6wwn EMDB-21941, PDB-6wwn: KIF14[391-748] - ADP-AlFx in complex with a microtubule Method: EM (helical sym.) / Resolution: 3.5 Å 21942 6wwo EMDB-21942, PDB-6wwo: KIF14[391-748] - AMP-PNP in complex with a microtubule Method: EM (helical sym.) / Resolution: 2.8 Å 21943 6wwp EMDB-21943, PDB-6wwp: Apo KIF14[391-743] in complex with a microtubule Method: EM (helical sym.) / Resolution: 3.1 Å 21944 6wwq EMDB-21944, PDB-6wwq: KIF14[391-743] - ADP in complex with a microtubule Method: EM (helical sym.) / Resolution: 3.0 Å 21945 6wwr EMDB-21945, PDB-6wwr: Kif14[391-743] - ADP-AlFx open state class in complex with a microtubule Method: EM (helical sym.) / Resolution: 2.7 Å 21946 6wws EMDB-21946, PDB-6wws: Kif14[391-743] - AMP-PNP open state class in complex with a microtubule Method: EM (helical sym.) / Resolution: 2.7 Å 21947 6wwt EMDB-21947, PDB-6wwt: Apo KIF14[391-735] in complex with a microtubule Method: EM (helical sym.) / Resolution: 3.2 Å 21948 6wwu EMDB-21948, PDB-6wwu: KIF14[391-735] - ADP-AlFx in complex with a microtubule Method: EM (helical sym.) / Resolution: 2.7 Å 21949 6wwv EMDB-21949, PDB-6wwv: KIF14[391-735] - ANP-PNP in complex with a microtubule Method: EM (helical sym.) / Resolution: 3.1 Å 23540 7lvq EMDB-23540, PDB-7lvq: KIF14[391-743] - AMP-PNP closed state class in complex with a microtubule Method: EM (helical sym.) / Resolution: 2.9 Å 23541 7lvr EMDB-23541, PDB-7lvr: KIF14[391-743] - ADP-AlFx closed state class in complex with a microtubule Method: EM (helical sym.) / Resolution: 2.9 Å
Chemicals	ChemComp-GTP: GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying moleculeYM ChemComp-MG: Unknown entry ChemComp-GDP: GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying moleculeYM ChemComp-TA1: TAXOL / medication, chemotherapyYM ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-AF3: ALUMINUM FLUORIDE ChemComp-ANP: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM
Source	mus musculus (house mouse) sus scrofa (pig)
Keywords	MOTOR PROTEIN / KIF14 / kinesin / motility / microtubule / tubulin