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

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 chemic...

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Detalles Bibliográficos
Autores principales: Qin, Jingyu, Zhang, Hui, Geng, Yizhao, Ji, Qing
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7555842/
https://www.ncbi.nlm.nih.gov/pubmed/32972035
http://dx.doi.org/10.3390/ijms21186977
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author Qin, Jingyu
Zhang, Hui
Geng, Yizhao
Ji, Qing
author_facet Qin, Jingyu
Zhang, Hui
Geng, Yizhao
Ji, Qing
author_sort Qin, Jingyu
collection PubMed
description 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.
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spelling pubmed-75558422020-10-19 How Kinesin-1 Utilize the Energy of Nucleotide: The Conformational Changes and Mechanochemical Coupling in the Unidirectional Motion of Kinesin-1 Qin, Jingyu Zhang, Hui Geng, Yizhao Ji, Qing Int J Mol Sci Review 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. MDPI 2020-09-22 /pmc/articles/PMC7555842/ /pubmed/32972035 http://dx.doi.org/10.3390/ijms21186977 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Qin, Jingyu
Zhang, Hui
Geng, Yizhao
Ji, Qing
How Kinesin-1 Utilize the Energy of Nucleotide: The Conformational Changes and Mechanochemical Coupling in the Unidirectional Motion of Kinesin-1
title How Kinesin-1 Utilize the Energy of Nucleotide: The Conformational Changes and Mechanochemical Coupling in the Unidirectional Motion of Kinesin-1
title_full How Kinesin-1 Utilize the Energy of Nucleotide: The Conformational Changes and Mechanochemical Coupling in the Unidirectional Motion of Kinesin-1
title_fullStr How Kinesin-1 Utilize the Energy of Nucleotide: The Conformational Changes and Mechanochemical Coupling in the Unidirectional Motion of Kinesin-1
title_full_unstemmed How Kinesin-1 Utilize the Energy of Nucleotide: The Conformational Changes and Mechanochemical Coupling in the Unidirectional Motion of Kinesin-1
title_short How Kinesin-1 Utilize the Energy of Nucleotide: The Conformational Changes and Mechanochemical Coupling in the Unidirectional Motion of Kinesin-1
title_sort how kinesin-1 utilize the energy of nucleotide: the conformational changes and mechanochemical coupling in the unidirectional motion of kinesin-1
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7555842/
https://www.ncbi.nlm.nih.gov/pubmed/32972035
http://dx.doi.org/10.3390/ijms21186977
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