1U2M
Crystal Structure of Skp
Summary for 1U2M
| Entry DOI | 10.2210/pdb1u2m/pdb |
| Descriptor | Histone-like protein HLP-1 (2 entities in total) |
| Functional Keywords | coiled coil, chaperone |
| Biological source | Escherichia coli |
| Cellular location | Periplasm : P0AEU7 |
| Total number of polymer chains | 3 |
| Total formula weight | 48556.27 |
| Authors | Walton, T.A.,Sousa, M.C. (deposition date: 2004-07-19, release date: 2004-08-24, Last modification date: 2024-11-13) |
| Primary citation | Walton, T.A.,Sousa, M.C. Crystal Structure of Skp, a Prefoldin-like Chaperone that Protects Soluble and Membrane Proteins from Aggregation Mol.Cell, 15:367-374, 2004 Cited by PubMed Abstract: 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. PubMed: 15304217DOI: 10.1016/j.molcel.2004.07.023 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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