TY - JOUR
T1 - Structural identification of DnaK binding sites within bovine and sheep bactenecin Bac7
AU - Zahn, Michael
AU - Kieslich, Björn
AU - Berthold, Nicole
AU - Knappe, Daniel
AU - Hoffmann, Ralf
AU - Sträter, Norbert
PY - 2014/4/1
Y1 - 2014/4/1
N2 - 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.
AB - 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.
KW - Antimicrobial peptide
KW - Chaperone
KW - Peptide binding mode
KW - X-ray crystallography
UR - http://www.scopus.com/inward/record.url?scp=84896349963&partnerID=8YFLogxK
U2 - 10.2174/09298665113206660111
DO - 10.2174/09298665113206660111
M3 - Article
C2 - 24164259
AN - SCOPUS:84896349963
SN - 0929-8665
VL - 21
SP - 407
EP - 412
JO - Protein and Peptide Letters
JF - Protein and Peptide Letters
IS - 4
ER -