Protein conformational exchanges modulated by the environment of outer membrane vesicles

Authors

  • Lichun He University of Chinese Academy of Sciences & State Key Laboratory of Magnetic Resonance and Atomic Molecular Physics, National Center for Magnetic Reso-nance in Wuhan, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences ,
  • Maili Liu State Key Laboratory of Magnetic Resonance and Atomic Molecular Physics, National Center for Magnetic Reso-nance in Wuhan, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences & University of Chinese Academy of Sciences & Optics Valley Laboratory ,
  • Guan Wang University of Chinese Academy of Sciences & State Key Laboratory of Magnetic Resonance and Atomic Molecular Physics, National Center for Magnetic Reso-nance in Wuhan, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences ,
  • Gangjin Yu State Key Laboratory of Magnetic Resonance and Atomic Molecular Physics, National Center for Magnetic Reso-nance in Wuhan, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences & University of Chinese Academy of Sciences ,
  • Dawei Gao State Key Laboratory of Metastable Materials Science and Technology, Nano-biotechnology Key Lab of Hebei Province, Applying Chemistry Key Lab of Hebei Province, Heavy Metal Deep-Remediation in Water and Resource Reuse Key Lab of Hebei, Yanshan University ,
  • Guosheng Jiang Department of Immunology, Binzhou Medical University ,
  • Huan Wang School of Life Science and Technology, Weifang Medical University ,
  • Tairan Yuwen Department of Pharmaceutical Analysis & State Key Laboratory of Natural and Biomimetic Drugs, School of Pharmaceutical Sciences, Peking University ,
  • Xu Zhang Zhang University of Chinese Academy of Sciences & State Key Laboratory of Magnetic Resonance and Atomic Molecular Physics, National Center for Magnetic Reso-nance in Wuhan, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences ,
  • Conggang Li State Key Laboratory of Magnetic Resonance and Atomic Molecular Physics, National Center for Magnetic Reso-nance in Wuhan, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences & University of Chinese Academy of Sciences ,
  • Daiwen Yang Department of Biological Sciences, National University of Singapore

Abstract

Protein function, in many cases, is highly related to its frustration status and hence intimately coupled to the dynamics and conformational equilibria of the protein. The environment surrounding proteins is critical for their dynamics and can dra-matically affect the conformational equilibria and subsequently activities of proteins. However, it is yet unclear how protein conformational equilibria are modulated by their crowded native environments. Here we revealed the immunity protein Im7 was less frustrated and shifted toward its ground state in OMVs than in the aqueous solution. Further experiments showed both macromolecular crowding and quinary interactions with the periplasmic components stabilized the ground state of Im7. Our studies highlight the key role of the OMVs environment played on protein conformational equilibria and subsequently conformation-related protein functions. Furthermore, the long-lasting NMR measurement time of proteins within OMVs underlies it could serve as a promising system to investigate protein structures and dynamics in situ via nuclear magnetic spectroscopy.

Content

Supplementary material

Methods and Materials
quantification by ImageJ, HSQC spectra, correlation between |Δω| in different conditions, solvent PRE, 15N CPMG RD profiles, and the plot of difference of βˆ†π‘…2,𝑒𝑓𝑓