The Periplasmic Chaperones Skp and SurA

Subcell Biochem. 2019:92:169-186. doi: 10.1007/978-3-030-18768-2_6.


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.

Keywords: Gram-negative bacteria; Molecular chaperones; Periplasm; Protein dynamics; Protein folding; Protein structure.

Publication types

  • Review

MeSH terms

  • Carrier Proteins / chemistry*
  • Carrier Proteins / metabolism*
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / metabolism*
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / metabolism*
  • Gram-Negative Bacteria / enzymology
  • Gram-Negative Bacteria / metabolism*
  • Molecular Chaperones / chemistry*
  • Molecular Chaperones / metabolism*
  • Peptidylprolyl Isomerase / chemistry*
  • Peptidylprolyl Isomerase / metabolism*
  • Periplasm / metabolism*


  • Carrier Proteins
  • DNA-Binding Proteins
  • Escherichia coli Proteins
  • Molecular Chaperones
  • Skp protein, E coli
  • SurA protein, E coli
  • Peptidylprolyl Isomerase