Structural Identification of DnaK Binding Sites within Bovine and Sheep Bactenecin Bac7

Author(s): Michael Zahn, Bjorn Kieslich, Nicole Berthold, Daniel Knappe, Ralf Hoffmann, Norbert Strater.

Journal Name: Protein & Peptide Letters

Volume 21 , Issue 4 , 2014


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.

Keywords: Antimicrobial peptide, chaperone, peptide binding mode, X-ray crystallography.

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Article Details

Year: 2014
Page: [407 - 412]
Pages: 6
DOI: 10.2174/09298665113206660111
Price: $58

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