Crystal Structure of Skp, a Prefoldin-like Chaperone that Protects Soluble and Membrane Proteins from Aggregation
| Autor: | Marcelo C. Sousa, Troy A. Walton |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
Lipopolysaccharides
Protein Folding Time Factors Membrane lipids Molecular Sequence Data Crystallography X-Ray Adenosine Triphosphate Escherichia coli Amino Acid Sequence Molecular Biology Binding Sites biology Escherichia coli Proteins Cell Biology Periplasmic space Protein Structure Tertiary Prefoldin DNA-Binding Proteins Cytosol Membrane Membrane protein Biochemistry Chaperone (protein) biology.protein Biophysics Bacterial outer membrane Bacterial Outer Membrane Proteins Molecular Chaperones |
| Zdroj: | Molecular Cell. 15:367-374 |
| ISSN: | 1097-2765 |
| DOI: | 10.1016/j.molcel.2004.07.023 |
| Popis: | The Seventeen Kilodalton Protein (Skp) is a trimeric periplasmic chaperone that assists outer membrane proteins in their folding and insertion into membranes. Here we report the crystal structure of Skp from E. coli. The structure of the Skp trimer resembles a jellyfish with alpha-helical tentacles protruding from a beta barrel body defining a central cavity. The architecture of Skp is unexpectedly similar to that of Prefoldin/GimC, a cytosolic chaperone present in eukaria and archea, that binds unfolded substrates in its central cavity. The ability of Skp to prevent the aggregation of model substrates in vitro is independent of ATP. Skp can interact directly with membrane lipids and lipopolysaccharide (LPS). These interactions are needed for efficient Skp-assisted folding of membrane proteins. We have identified a putative LPS binding site on the outer surface of Skp and propose a model for unfolded substrate binding. |
| Databáze: | OpenAIRE |
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