1sg2
From Proteopedia
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Crystal structure of the periplasmic chaperone Skp
Overview
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.
About this Structure
1SG2 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture., Korndorfer IP, Dommel MK, Skerra A, Nat Struct Mol Biol. 2004 Oct;11(10):1015-20. Epub 2004 Sep 12. PMID:15361861
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