PDBsum entry 4jwc

Chaperone/antibiotic

PDB id: 4jwc

Contents

Protein chains

213 a.a.

Ligands

ARG-PRO-PRO-ARG-LEU-PRO-ARG-PRO-ARG

ARG-PRO-PRO-ARG-LEU-PRO-ARG-PRO-ARG-PRO

SO4 ×3

Waters ×372

References listed in PDB file

Key reference

• Title: Structural identification of dnak binding sites within bovine and sheep bactenecin bac7.
• Authors: M.Zahn, B.Kieslich, N.Berthold, D.Knappe, R.Hoffmann, N.Strater.
• Ref.: Protein Pept Lett, 2014, 21, 407-412.
• PubMed id: 24164259

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.