4JWI

Crystal structure of the substrate binding domain of E.coli DnaK in complex with sheep Bac7(35-43)

Summary for 4JWI

• Entry DOI: 10.2210/pdb4jwi/pdb
• Related: 1DKX 1DKY 1DKZ 3DPO 3DPP 3DPQ 3QNJ 4E81 4JWC 4JWD 4JWE
• Descriptor: Chaperone protein DnaK, Cathelicidin-3, SULFATE ION, ... (4 entities in total)
• Functional Keywords: chaperone, peptide binding, antimicrobial peptide, chaperone-antibiotic complex, chaperone/antibiotic
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm : P0A6Y8; Secreted: P50415
• Total number of polymer chains: 4
• Total formula weight: 50416.74

Authors

Zahn, M.,Straeter, N. (deposition date: 2013-03-27, release date: 2013-11-13, Last modification date: 2023-09-20)

Primary citation

Zahn, M.,Kieslich, B.,Berthold, N.,Knappe, D.,Hoffmann, R.,Strater, N.
Structural Identification of DnaK Binding Sites within Bovine and Sheep Bactenecin Bac7.
Protein Pept.Lett., 21:407-412, 2014

PubMed 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.

PubMed: 24164259

Experimental method

X-RAY DIFFRACTION (1.9 Å)