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

IUCrJ

Niebling, S.¹  Gao, Y.²  Josts, I.³  Levantino, M.⁴ 

[1] The Department of Chemistry, The University of Hamburg, Hamburg 20146, Germany;The Department of Physics, The University of Hamburg, Hamburg 20355, Germany;The Hamburg Center for Ultrafast Imaging, University of Hamburg, Hamburg 22761, Germany;The Max Planck Institute for the Structure and Dynamics of Matter, Hamburg 22761, Germany

关键词: BIOPHYSICS;    X-RAY SOLUTION SCATTERING;    PHOTOCAGING;    STRUCTURAL BIOLOGY;   

DOI  :  10.1107/S2052252518012149

学科分类：数学（综合）

来源: International Union of Crystallography

【 摘 要 】

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.

【 授权许可】

CC BY