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

PDB id:

4jwc

Name:

Chaperone/antibiotic

Title:

Crystal structure of the substrate binding domain of e.Coli dnak in complex with bovine bac7(1-16)

Structure:

Chaperone protein dnak. Chain: a, b. Fragment: uno residues 389-607. Synonym: hsp70, heat shock 70 kda protein, heat shock protein 70. Engineered: yes. Cathelicidin-3. Chain: c, d. Fragment: unp residues 131-146. Synonym: bactenecin-7, bac7, pr-59.

Source:

Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: dnak, grop, grpf, seg. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Bos taurus. Cow.

Resolution:

1.80Å R-factor: 0.203 R-free: 0.225

Authors:

M.Zahn,N.Straeter

Key ref:

M.Zahn et al. (2014). Structural identification of DnaK binding sites within bovine and sheep bactenecin Bac7. Protein Pept Lett, 21, 407-412. PubMed id: 24164259

Date:

27-Mar-13 Release date: 13-Nov-13

Protein chains

P0A6Y8  (DNAK_ECOLI) -  Chaperone protein DnaK from Escherichia coli (strain K12)

Seq: 638 a.a.

Struc: 213 a.a.

Protein Pept Lett 21:407-412 (2014)

PubMed id: 24164259

Structural identification of DnaK binding sites within bovine and sheep bactenecin Bac7.

M.Zahn, B.Kieslich, N.Berthold, D.Knappe, R.Hoffmann, N.Strater.

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.