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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
Descripción
Sumario: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.