Litcius/Paper detail

How Kinesin-1 Utilize the Energy of Nucleotide: The Conformational Changes and Mechanochemical Coupling in the Unidirectional Motion of Kinesin-1

Jingyu Qin, Hui Zhang, Yi-Zhao Geng, Qing Ji

2020International Journal of Molecular Sciences25 citationsDOIOpen Access PDF

Abstract

Kinesin-1 is a typical motile molecular motor and the founding member of the kinesin family. The most significant feature in the unidirectional motion of kinesin-1 is its processivity. To realize the fast and processive movement on the microtubule lattice, kinesin-1 efficiently transforms the chemical energy of nucleotide binding and hydrolysis to the energy of mechanical movement. The chemical and mechanical cycle of kinesin-1 are coupled to avoid futile nucleotide hydrolysis. In this paper, the research on the mechanical pathway of energy transition and the regulating mechanism of the mechanochemical cycle of kinesin-1 is reviewed.

Topics & Concepts

KinesinProcessivityMicrotubuleChemical energyATP hydrolysisBiophysicsMolecular motorChemistryMotor proteinNucleotideMechanochemistryCoupling (piping)Mechanical energyCell biologyPhysicsBiologyBiochemistryMaterials scienceDNAEnzymePower (physics)GeneMetallurgyOrganic chemistryQuantum mechanicsDNA replicationATPaseMicrotubule and mitosis dynamicsCellular Mechanics and InteractionsCellular transport and secretion
How Kinesin-1 Utilize the Energy of Nucleotide: The Conformational Changes and Mechanochemical Coupling in the Unidirectional Motion of Kinesin-1 | Litcius