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Design principles governing chemomechanical coupling of kinesin

A systematic chemomechanical network model for the molecular motor kinesin is presented in this report. The network model is based on the nucleotide-dependent binding affinity of the heads to an microtubule (MT) and the asymmetries and similarities between the chemical transitions caused by the intr...

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Autor principal: Sumi, Tomonari
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5430765/
https://www.ncbi.nlm.nih.gov/pubmed/28442770
http://dx.doi.org/10.1038/s41598-017-01328-9
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author Sumi, Tomonari
author_facet Sumi, Tomonari
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description A systematic chemomechanical network model for the molecular motor kinesin is presented in this report. The network model is based on the nucleotide-dependent binding affinity of the heads to an microtubule (MT) and the asymmetries and similarities between the chemical transitions caused by the intramolecular strain between the front and rear heads. The network model allows for multiple chemomechanical cycles and takes into account all possible mechanical transitions between states in which one head is strongly bound and the other head is weakly bound to an MT. The results obtained from the model show the ATP-concentration dependence of the dominant forward stepping cycle and support a gated rear head mechanism in which the forward step is controlled by ATP hydrolysis and the resulting ADP-bound state of the rear head when the ATP level is saturated. When the ATP level is saturated, the energy from ATP hydrolysis is used to concentrate the chemical transition flux to a force-generating state that can produce the power stroke. In contrast, when the ATP level is low, the hydrolysis energy is consumed to avoid states in which the leading head is weakly bound to an MT and to inhibit frequent backward steps upon loading.
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spelling pubmed-54307652017-05-16 Design principles governing chemomechanical coupling of kinesin Sumi, Tomonari Sci Rep Article A systematic chemomechanical network model for the molecular motor kinesin is presented in this report. The network model is based on the nucleotide-dependent binding affinity of the heads to an microtubule (MT) and the asymmetries and similarities between the chemical transitions caused by the intramolecular strain between the front and rear heads. The network model allows for multiple chemomechanical cycles and takes into account all possible mechanical transitions between states in which one head is strongly bound and the other head is weakly bound to an MT. The results obtained from the model show the ATP-concentration dependence of the dominant forward stepping cycle and support a gated rear head mechanism in which the forward step is controlled by ATP hydrolysis and the resulting ADP-bound state of the rear head when the ATP level is saturated. When the ATP level is saturated, the energy from ATP hydrolysis is used to concentrate the chemical transition flux to a force-generating state that can produce the power stroke. In contrast, when the ATP level is low, the hydrolysis energy is consumed to avoid states in which the leading head is weakly bound to an MT and to inhibit frequent backward steps upon loading. Nature Publishing Group UK 2017-04-25 /pmc/articles/PMC5430765/ /pubmed/28442770 http://dx.doi.org/10.1038/s41598-017-01328-9 Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Sumi, Tomonari
Design principles governing chemomechanical coupling of kinesin
title Design principles governing chemomechanical coupling of kinesin
title_full Design principles governing chemomechanical coupling of kinesin
title_fullStr Design principles governing chemomechanical coupling of kinesin
title_full_unstemmed Design principles governing chemomechanical coupling of kinesin
title_short Design principles governing chemomechanical coupling of kinesin
title_sort design principles governing chemomechanical coupling of kinesin
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5430765/
https://www.ncbi.nlm.nih.gov/pubmed/28442770
http://dx.doi.org/10.1038/s41598-017-01328-9
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