The periplasmic E. coli chaperone Skp is a trimer in solution: Biophysical and preliminary crystallographic characterization

Martin Schlapschy, Monica K. Dommel, Kamyar Hadian, Marton Fogarasi, Ingo P. Korndörfer, Arne Skerra

Research output: Contribution to journalArticlepeer-review

31 Scopus citations

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 Å resolution.

Original languageEnglish
Pages (from-to)137-143
Number of pages7
JournalBiological Chemistry
Volume385
Issue number2
DOIs
StatePublished - Feb 2004

Keywords

  • Circular dichroism
  • Cross-linking
  • Outer membrane protein
  • Protein folding
  • Strep-tag
  • Thermal denaturation

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