Crystallization and preliminary X-ray crystallographic studies of an oligomeric species of a refolded C39 peptidase-like domain of the Escherichia coli ABC transporter haemolysin B

Christian K.W. Schwarz, Britta Tschapek, Thorsten Jumpertz, Stefan Jenewein, Justin Lecher, Dieter Willbold, Santosh Panjikar, I. Barry Holland, Sander H.J. Smits, Lutz Schmitt

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Abstract

The ABC transporter haemolysin B (HlyB) from Escherichia coli is part of a type I secretion system that translocates a 110 kDa toxin in one step across both membranes of this Gram-negative bacterium in an ATP-dependent manner. Sequence analysis indicates that HlyB contains a C39 peptidase-like domain at its N-terminus. C39 domains are thiol-dependent peptidases that cleave their substrates after a GG motif. Interestingly, the catalytically invariant cysteine is replaced by a tyrosine in the C39-like domain of HlyB. Here, the overexpression, purification and crystallization of the isolated C39-like domain are described as a first step towards obtaining structural insights into this domain and eventually answering the question concerning the function of a degenerated C39 domain in the ABC transporter HlyB.

Original languageEnglish
Pages (from-to)630-633
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume67
Issue number5
DOIs
Publication statusPublished - May 2011
Externally publishedYes

Keywords

  • buffer screens
  • C39 peptidases
  • haemolysins
  • inclusion bodies
  • oligomers
  • refolding
  • type I secretion systems

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