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cpSRP43 Is Both Highly Flexible and Stable: Structural Insights Using a Combined Experimental and Computational Approach
[Image: see text] The novel multidomain protein, cpSRP43, is a unique subunit of the post-translational chloroplast signal recognition particle (cpSRP) targeting pathway in higher plants. The cpSRP pathway is responsible for targeting and insertion of light-harvesting chlorophyll a/b binding protein...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2023
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10336970/ https://www.ncbi.nlm.nih.gov/pubmed/37336508 http://dx.doi.org/10.1021/acs.jcim.3c00319 |
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author | Benton, Mitchell Furr, Mercede Govind Kumar, Vivek Polasa, Adithya Gao, Feng Heyes, Colin David Suresh Kumar, Thallapuranam Krishnaswamy Moradi, Mahmoud |
author_facet | Benton, Mitchell Furr, Mercede Govind Kumar, Vivek Polasa, Adithya Gao, Feng Heyes, Colin David Suresh Kumar, Thallapuranam Krishnaswamy Moradi, Mahmoud |
author_sort | Benton, Mitchell |
collection | PubMed |
description | [Image: see text] The novel multidomain protein, cpSRP43, is a unique subunit of the post-translational chloroplast signal recognition particle (cpSRP) targeting pathway in higher plants. The cpSRP pathway is responsible for targeting and insertion of light-harvesting chlorophyll a/b binding proteins (LHCPs) to the thylakoid membrane. Upon emergence into the stroma, LHCPs form a soluble transit complex with the cpSRP heterodimer, which is composed of cpSRP43 and cpSRP54. cpSRP43 is irreplaceable as a chaperone to LHCPs in their translocation to the thylakoid membrane and remarkable in its ability to dissolve aggregates of LHCPs without the need for external energy input. In previous studies, cpSRP43 has demonstrated significant flexibility and interdomain dynamics. In this study, we explore the structural stability and flexibility of cpSRP43 using a combination of computational and experimental techniques and find that this protein is concurrently highly stable and flexible. In addition to microsecond-level unbiased molecular dynamics (MD), biased MD simulations based on system-specific collective variables are used along with biophysical experimentation to explain the basis of the flexibility and stability of cpSRP43, showing that the free and cpSRP54-bound cpSRP43 has substantially different conformations and conformational dynamics. |
format | Online Article Text |
id | pubmed-10336970 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-103369702023-07-13 cpSRP43 Is Both Highly Flexible and Stable: Structural Insights Using a Combined Experimental and Computational Approach Benton, Mitchell Furr, Mercede Govind Kumar, Vivek Polasa, Adithya Gao, Feng Heyes, Colin David Suresh Kumar, Thallapuranam Krishnaswamy Moradi, Mahmoud J Chem Inf Model [Image: see text] The novel multidomain protein, cpSRP43, is a unique subunit of the post-translational chloroplast signal recognition particle (cpSRP) targeting pathway in higher plants. The cpSRP pathway is responsible for targeting and insertion of light-harvesting chlorophyll a/b binding proteins (LHCPs) to the thylakoid membrane. Upon emergence into the stroma, LHCPs form a soluble transit complex with the cpSRP heterodimer, which is composed of cpSRP43 and cpSRP54. cpSRP43 is irreplaceable as a chaperone to LHCPs in their translocation to the thylakoid membrane and remarkable in its ability to dissolve aggregates of LHCPs without the need for external energy input. In previous studies, cpSRP43 has demonstrated significant flexibility and interdomain dynamics. In this study, we explore the structural stability and flexibility of cpSRP43 using a combination of computational and experimental techniques and find that this protein is concurrently highly stable and flexible. In addition to microsecond-level unbiased molecular dynamics (MD), biased MD simulations based on system-specific collective variables are used along with biophysical experimentation to explain the basis of the flexibility and stability of cpSRP43, showing that the free and cpSRP54-bound cpSRP43 has substantially different conformations and conformational dynamics. American Chemical Society 2023-06-19 /pmc/articles/PMC10336970/ /pubmed/37336508 http://dx.doi.org/10.1021/acs.jcim.3c00319 Text en © 2023 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by-nc-nd/4.0/Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Benton, Mitchell Furr, Mercede Govind Kumar, Vivek Polasa, Adithya Gao, Feng Heyes, Colin David Suresh Kumar, Thallapuranam Krishnaswamy Moradi, Mahmoud cpSRP43 Is Both Highly Flexible and Stable: Structural Insights Using a Combined Experimental and Computational Approach |
title | cpSRP43 Is Both
Highly Flexible and Stable: Structural
Insights Using a Combined Experimental and Computational Approach |
title_full | cpSRP43 Is Both
Highly Flexible and Stable: Structural
Insights Using a Combined Experimental and Computational Approach |
title_fullStr | cpSRP43 Is Both
Highly Flexible and Stable: Structural
Insights Using a Combined Experimental and Computational Approach |
title_full_unstemmed | cpSRP43 Is Both
Highly Flexible and Stable: Structural
Insights Using a Combined Experimental and Computational Approach |
title_short | cpSRP43 Is Both
Highly Flexible and Stable: Structural
Insights Using a Combined Experimental and Computational Approach |
title_sort | cpsrp43 is both
highly flexible and stable: structural
insights using a combined experimental and computational approach |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10336970/ https://www.ncbi.nlm.nih.gov/pubmed/37336508 http://dx.doi.org/10.1021/acs.jcim.3c00319 |
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