The Periplasmic Chaperones Skp and SurA

Mas, Guillaume and Thoma, Johannes and Hiller, Sebastian. (2019) The Periplasmic Chaperones Skp and SurA. In: Bacterial Cell Walls and Membranes, 92. Cham, pp. 169-186.

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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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Hiller)
UniBasel Contributors:Hiller Odermatt, Sebastian and Mas, Guillaume
Item Type:Book Section, refereed
Book Section Subtype:Further Contribution in a Book
Publisher:Springer Nature
Series Name:Subcellular Biochemistry
Issue Number:92
Note:Publication type according to Uni Basel Research Database: Book item
Identification Number:
Last Modified:24 Mar 2020 10:53
Deposited On:24 Mar 2020 10:53

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