4JWC

Crystal structure of the substrate binding domain of E.coli DnaK in complex with bovine Bac7(1-16)

4JWC の概要

• エントリーDOI: 10.2210/pdb4jwc/pdb
• 関連するPDBエントリー: 1DKX 1DKY 1DKZ 3DPO 3DPP 3DPQ 3QNJ 4E81 4JWD 4JWE 4JWI
• 分子名称: Chaperone protein DnaK, Cathelicidin-3, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: chaperone, peptide binding, antimicrobial peptide, peptide binding protein, chaperone-protein binding complex, chaperone-antibiotic complex, chaperone/antibiotic
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm : P0A6Y8; Secreted: P19661
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 52098.88

構造登録者

Zahn, M.,Straeter, N. (登録日: 2013-03-27, 公開日: 2013-11-13, 最終更新日: 2023-09-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.8 Å)