Abstract
The periplasm of Gram-negative bacteria contains a specialized chaperone network that facilitates the transport of unfolded membrane proteins to the outer membrane as its primary functional role. The network, involving the chaperones Skp and SurA as key players and potentially additional chaperones, is indispensable for the survival of the cell. Structural descriptions of the apo forms of these molecular chaperones were initially provided by X-ray crystallography. Subsequently, a combination of experimental biophysical methods including solution NMR spectroscopy provided a detailed understanding of full-length chaperone–client complexes . The data showed that conformational changes and dynamic re-organization of the chaperones upon client binding, as well as client dynamics on the chaperone surface are crucial for function. This chapter gives an overview of the structure-function relationship of the dynamic conformational rearrangements that regulate the functional cycles of the periplasmic molecular chaperones Skp and SurA.
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Abbreviations
- ATP:
-
Adenosine 5′-triphosphate
- BAM:
-
β-barrel assembly machinery
- Hsp60:
-
Heat shock protein 60
- NMR:
-
Nuclear magnetic resonance
- NOE:
-
Nuclear Overhauser effect
- OMP:
-
Outer membrane protein
- PPIase:
-
Parvulin-like peptidyl-prolyl isomerase
- PRE:
-
Paramagnetic relaxation enhancement
- SAXS:
-
Small angle X-ray scattering
- Skp:
-
Seventeen Kilodalton Protein
- SurA:
-
Survival factor A
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Acknowledgements
This work was supported by the Swiss National Science Foundation and the NFP 72 (grants 31003A_166426 and 407240_167125 to S.H.) and by the Swiss Nanoscience institute. The authors declare no conflict of interest.
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Mas, G., Thoma, J., Hiller, S. (2019). The Periplasmic Chaperones Skp and SurA. In: Kuhn, A. (eds) Bacterial Cell Walls and Membranes . Subcellular Biochemistry, vol 92. Springer, Cham. https://doi.org/10.1007/978-3-030-18768-2_6
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