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Photocage-initiated time-resolved solution X-ray scattering investigation of protein dimerization

This work demonstrates a new method for investigating time-resolved structural changes in protein conformation and oligomerization via photocage-initiated time-resolved X-ray solution scattering by observing the ATP-driven dimerization of the MsbA nucleotide-binding domain. Photocaged small molecule...

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Detalles Bibliográficos
Autores principales: Josts, Inokentijs, Niebling, Stephan, Gao, Yunyun, Levantino, Matteo, Tidow, Henning, Monteiro, Diana
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6211537/
https://www.ncbi.nlm.nih.gov/pubmed/30443351
http://dx.doi.org/10.1107/S2052252518012149
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author Josts, Inokentijs
Niebling, Stephan
Gao, Yunyun
Levantino, Matteo
Tidow, Henning
Monteiro, Diana
author_facet Josts, Inokentijs
Niebling, Stephan
Gao, Yunyun
Levantino, Matteo
Tidow, Henning
Monteiro, Diana
author_sort Josts, Inokentijs
collection PubMed
description This work demonstrates a new method for investigating time-resolved structural changes in protein conformation and oligomerization via photocage-initiated time-resolved X-ray solution scattering by observing the ATP-driven dimerization of the MsbA nucleotide-binding domain. Photocaged small molecules allow the observation of single-turnover reactions of non-naturally photoactivatable proteins. The kinetics of the reaction can be derived from changes in X-ray scattering associated with ATP-binding and subsequent dimerization. This method can be expanded to any small-molecule-driven protein reaction with conformational changes traceable by X-ray scattering where the small molecule can be photocaged.
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spelling pubmed-62115372018-11-15 Photocage-initiated time-resolved solution X-ray scattering investigation of protein dimerization Josts, Inokentijs Niebling, Stephan Gao, Yunyun Levantino, Matteo Tidow, Henning Monteiro, Diana IUCrJ Research Letters This work demonstrates a new method for investigating time-resolved structural changes in protein conformation and oligomerization via photocage-initiated time-resolved X-ray solution scattering by observing the ATP-driven dimerization of the MsbA nucleotide-binding domain. Photocaged small molecules allow the observation of single-turnover reactions of non-naturally photoactivatable proteins. The kinetics of the reaction can be derived from changes in X-ray scattering associated with ATP-binding and subsequent dimerization. This method can be expanded to any small-molecule-driven protein reaction with conformational changes traceable by X-ray scattering where the small molecule can be photocaged. International Union of Crystallography 2018-09-13 /pmc/articles/PMC6211537/ /pubmed/30443351 http://dx.doi.org/10.1107/S2052252518012149 Text en © Inokentijs Josts et al. 2018 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.http://creativecommons.org/licenses/by/2.0/uk/
spellingShingle Research Letters
Josts, Inokentijs
Niebling, Stephan
Gao, Yunyun
Levantino, Matteo
Tidow, Henning
Monteiro, Diana
Photocage-initiated time-resolved solution X-ray scattering investigation of protein dimerization
title Photocage-initiated time-resolved solution X-ray scattering investigation of protein dimerization
title_full Photocage-initiated time-resolved solution X-ray scattering investigation of protein dimerization
title_fullStr Photocage-initiated time-resolved solution X-ray scattering investigation of protein dimerization
title_full_unstemmed Photocage-initiated time-resolved solution X-ray scattering investigation of protein dimerization
title_short Photocage-initiated time-resolved solution X-ray scattering investigation of protein dimerization
title_sort photocage-initiated time-resolved solution x-ray scattering investigation of protein dimerization
topic Research Letters
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6211537/
https://www.ncbi.nlm.nih.gov/pubmed/30443351
http://dx.doi.org/10.1107/S2052252518012149
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