Abstract
The periplasmic chaperone SurA in Gram-negative bacteria plays a central role in the biogenesis of integral outer membrane proteins and is critical to the maintenance of bacterial membrane integrity. SurA contains a core chaperone module comprising the N- and C-terminal domains, along with two peptidyl-prolyl isomerase (PPIase) domains. The chaperone activity of SurA has been demonstrated to rely on the core module, whereas recent works suggested that the PPIase domains may regulate the chaperone activity through large conformational rearrangements. Herein, we report the resonance assignments of 1H, 13C and 15N atoms of the second PPIase domain of Escherichia coli SurA, which provide valuable information for further studies of the structure, dynamics and interactions of this chaperone using NMR techniques.
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Acknowledgements
All NMR experiments were carried out at the Beijing NMR Center. We thank Dr. Hongwei Li at Beijing NMR Center for assistance in NMR data collection. This work was supported by Grant 31370718 from the National Natural Science Foundation of China to Y. H. and Grant 2016YFA0501201 from the National Key R&D Program of China to C. J.
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Jia, M., Hu, Y. & Jin, C. 1H, 13C and 15N resonance assignments of the second peptidyl-prolyl isomerase domain of chaperone SurA from Escherichia coli. Biomol NMR Assign 13, 183–186 (2019). https://doi.org/10.1007/s12104-019-09874-1
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DOI: https://doi.org/10.1007/s12104-019-09874-1