Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture

Abstract

The 17-kDa protein (Skp) of Escherichia coli is a homotrimeric periplasmic chaperone for newly synthesized outer-membrane proteins. Here we present its X-ray structure at a resolution of 2.35 Å. Three hairpin-shaped α-helical extensions reach out by ∼60 Å from a trimerization domain, which is composed of three intersubunit β-sheets that wind around a… (More)
DOI: 10.1038/nsmb828

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@article{Korndrfer2004StructureOT, title={Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture}, author={Ingo P Kornd{\"o}rfer and Monica K Dommel and Arne Skerra}, journal={Nature Structural &Molecular Biology}, year={2004}, volume={11}, pages={1015-1020} }