Structural identification of DnaK binding sites within bovine and sheep bactenecin Bac7

Michael Zahn, Björn Kieslich, Nicole Berthold, Daniel Knappe, Ralf Hoffmann, Norbert Sträter*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Bacterial resistance against common antibiotics is an increasing health problem. New pharmaceuticals for the treatment of infections caused by resistant pathogens are needed. Small proline-rich antimicrobial peptides (PrAMPs) from insects are known to bind intracellularly to the conventional substrate binding cleft of the E. coli Hsp70 chaperone DnaK. Furthermore, bactenecins from mammals, members of the cathelicidin family, also contain potential DnaK binding sites. Crystal structures of bovine and sheep Bac7 in complex with the DnaK substrate binding domain show that the peptides bind in the forward binding mode with a leucine positioned in the central hydrophobic pocket. In most structures, proline and arginine residues preceding leucine occupy the hydrophobic DnaK binding sites -1 and -2. Within bovine Bac7, four potential DnaK binding sites were identified.

Original languageEnglish
Pages (from-to)407-412
Number of pages6
JournalProtein and Peptide Letters
Issue number4
Publication statusPublished - 1 Apr 2014


  • Antimicrobial peptide
  • Chaperone
  • Peptide binding mode
  • X-ray crystallography


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