PMID:15361861
| Citation |
Korndörfer, IP, Dommel, MK and Skerra, A (2004) Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture. Nat. Struct. Mol. Biol. 11:1015-20 |
|---|---|
| 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 A. Three hairpin-shaped alpha-helical extensions reach out by approximately 60 A from a trimerization domain, which is composed of three intersubunit beta-sheets that wind around a central axis. The alpha-helical extensions approach each other at their distal turns, resulting in a fold that resembles a 'three-pronged grasping forceps'. The overall shape of Skp is reminiscent of the cytosolic chaperone prefoldin, although it is based on a radically different topology. The peculiar architecture, with apparent plasticity of the prongs and distinct electrostatic and hydrophobic surface properties, supports the recently proposed biochemical mechanism of this chaperone: formation of a Skp(3)-Omp complex protects the outer membrane protein from aggregation during passage through the bacterial periplasm. |
| Links |
PubMed Online version:10.1038/nsmb828 |
| Keywords |
Amino Acid Sequence; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/physiology; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/physiology; Models, Molecular; Molecular Chaperones/chemistry; Molecular Chaperones/physiology; Molecular Sequence Data; Periplasm/metabolism; Protein Structure, Quaternary; Sequence Homology, Amino Acid; Surface Properties |
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