PMID:15101556
| Citation |
Schlapschy, M, Dommel, MK, Hadian, K, Fogarasi, M, Korndörfer, IP and Skerra, A (2004) The periplasmic E. coli chaperone Skp is a trimer in solution: biophysical and preliminary crystallographic characterization. Biol. Chem. 385:137-43 |
|---|---|
| Abstract |
The 'seventeen kilodalton protein' Skp confers transient solubility on outer membrane proteins during biogenesis in Gram-negative bacteria. Here we report a first biophysical characterization of this chaperone itself, which also possesses biotechnological potential in the production of recombinant proteins. Using cross-linking and gel filtration methods, we found that Skp forms a stable homo-trimer in solution. Following thermal denaturation, monitored by CD spectroscopy, this chaperone refolds with high efficiency but exhibits a pronounced hysteresis between the un- and refolding transitions. Using the recombinant protein equipped with the Strep-tag II at its N-terminus, suitable crystallization conditions for Skp were found. A first data set was collected to 2.60 A resolution. |
| Links |
PubMed Online version:10.1515/BC.2004.032 |
| Keywords |
Amino Acid Sequence; Circular Dichroism; Crystallization; Crystallography, X-Ray; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Hot Temperature; Molecular Chaperones/chemistry; Molecular Chaperones/genetics; Molecular Sequence Data; Periplasm/metabolism; Periplasmic Proteins/chemistry; Periplasmic Proteins/genetics; Protein Denaturation; Protein Renaturation; Protein Structure, Quaternary; Protein Structure, Secondary; Recombinant Proteins/chemistry; Recombinant Proteins/genetics |
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