期刊
NATURE COMMUNICATIONS
卷 11, 期 1, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-020-15702-1
关键词
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资金
- BBSRC [BB/P000037/1, BB/N007603/1, BB/T000635/1, BB/N017307/1, BB/M011151/1]
- EPSRC [EP/N035267/1, BB/M012573/1]
- US National Institutes of Health [GM102829]
- MRC [MR/P018491/1]
- Wellcome Trust [105615/Z/14/Z, 208385/Z/17/Z]
- BBSRC [BB/T000635/1, BB/N017307/1, BB/N007603/1, BB/P000037/1, BB/M012573/1] Funding Source: UKRI
- EPSRC [EP/N035267/1] Funding Source: UKRI
- MRC [MR/P018491/1] Funding Source: UKRI
- Wellcome Trust [208385/Z/17/Z] Funding Source: Wellcome Trust
The periplasmic chaperone SurA plays a key role in outer membrane protein (OMP) biogenesis. E. coli SurA comprises a core domain and two peptidylprolyl isomerase domains (P1 and P2), but its mechanisms of client binding and chaperone function have remained unclear. Here, we use chemical cross-linking, hydrogen-deuterium exchange mass spectrometry, single-molecule FRET and molecular dynamics simulations to map the client binding site(s) on SurA and interrogate the role of conformational dynamics in OMP recognition. We demonstrate that SurA samples an array of conformations in solution in which P2 primarily lies closer to the core/P1 domains than suggested in the SurA crystal structure. OMP binding sites are located primarily in the core domain, and OMP binding results in conformational changes between the core/P1 domains. Together, the results suggest that unfolded OMP substrates bind in a cradle formed between the SurA domains, with structural flexibility between domains assisting OMP recognition, binding and release. The chaperone SurA is involved in outer membrane protein (OMP) biogenesis in Gram-negative bacteria, but its mechanism of action is not fully understood. Combining mass spectrometric, biophysical and computational approaches, the authors here show how the conformational dynamics of SurA facilitate OMP binding.
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