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

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

Volume: 21 Issue: 4

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

Affiliation:

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

Abstract: 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.

Cite this article as:

Zahn Michael, Kieslich Bjorn, Berthold Nicole, Knappe Daniel, Hoffmann Ralf and Strater Norbert, Structural Identification of DnaK Binding Sites within Bovine and Sheep Bactenecin Bac7, Protein & Peptide Letters 2014; 21 (4) . https://dx.doi.org/10.2174/09298665113206660111

DOI https://dx.doi.org/10.2174/09298665113206660111	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305