1u2m

Crystal Structure of SkpCrystal Structure of Skp

Structural highlights

1u2m is a 3 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SKP_ECOLI Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm. Required for the efficient release of OmpA from the inner membrane, the maintenance of its solubility in the periplasm, and, in association with lipopolysaccharide (LPS), for the efficient folding and insertion of OmpA into the outer membrane.^[1] ^[2] ^[3] ^[4] ^[5]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ Chen R, Henning U. A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins. Mol Microbiol. 1996 Mar;19(6):1287-94. PMID:8730870
↑ De Cock H, Schafer U, Potgeter M, Demel R, Muller M, Tommassen J. Affinity of the periplasmic chaperone Skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins. Role of Skp in the biogenesis of outer membrane protein. Eur J Biochem. 1999 Jan;259(1-2):96-103. PMID:9914480
↑ Schafer U, Beck K, Muller M. Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins. J Biol Chem. 1999 Aug 27;274(35):24567-74. PMID:10455120
↑ Harms N, Koningstein G, Dontje W, Muller M, Oudega B, Luirink J, de Cock H. The early interaction of the outer membrane protein phoe with the periplasmic chaperone Skp occurs at the cytoplasmic membrane. J Biol Chem. 2001 Jun 1;276(22):18804-11. Epub 2001 Mar 5. PMID:11278858 doi:http://dx.doi.org/10.1074/jbc.M011194200
↑ Bulieris PV, Behrens S, Holst O, Kleinschmidt JH. Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide. J Biol Chem. 2003 Mar 14;278(11):9092-9. Epub 2002 Dec 30. PMID:12509434 doi:http://dx.doi.org/10.1074/jbc.M211177200

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OCA

[1] Chen R, Henning U. A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins. Mol Microbiol. 1996 Mar;19(6):1287-94. PMID:8730870

[2] De Cock H, Schafer U, Potgeter M, Demel R, Muller M, Tommassen J. Affinity of the periplasmic chaperone Skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins. Role of Skp in the biogenesis of outer membrane protein. Eur J Biochem. 1999 Jan;259(1-2):96-103. PMID:9914480

[3] Schafer U, Beck K, Muller M. Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins. J Biol Chem. 1999 Aug 27;274(35):24567-74. PMID:10455120

[4] Harms N, Koningstein G, Dontje W, Muller M, Oudega B, Luirink J, de Cock H. The early interaction of the outer membrane protein phoe with the periplasmic chaperone Skp occurs at the cytoplasmic membrane. J Biol Chem. 2001 Jun 1;276(22):18804-11. Epub 2001 Mar 5. PMID:11278858 doi:http://dx.doi.org/10.1074/jbc.M011194200

[5] Bulieris PV, Behrens S, Holst O, Kleinschmidt JH. Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide. J Biol Chem. 2003 Mar 14;278(11):9092-9. Epub 2002 Dec 30. PMID:12509434 doi:http://dx.doi.org/10.1074/jbc.M211177200

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