3DPQ

Crystal structure of the substrate binding domain of E. coli DnaK in complex with a long pyrrhocoricin-derived inhibitor peptide (form B)

3DPQ の概要

• エントリーDOI: 10.2210/pdb3dpq/pdb
• 分子名称: Chaperone protein dnaK, inhibitor peptide, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: molecular chaperone, dnak, hsp70, substrate-binding domain, pyrrhocoricin inhibitor, atp-binding, chaperone, cytoplasm, dna replication, membrane, nucleotide-binding, phosphoprotein, stress response, peptide binding protein
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm: P0A6Y8
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 105246.85

構造登録者

Roujeinikova, A. (登録日: 2008-07-09, 公開日: 2009-03-10, 最終更新日: 2024-11-13)

主引用文献

Liebscher, M.,Roujeinikova, A.
Allosteric coupling between the lid and interdomain linker in DnaK revealed by inhibitor binding studies.
J.Bacteriol., 191:1456-1462, 2009

PubMed Abstract: The molecular chaperone DnaK assists protein folding and refolding, translocation across membranes, and regulation of the heat shock response. In Escherichia coli, the protein is a target for insect-derived antimicrobial peptides, pyrrhocoricins. We present here the X-ray crystallographic analysis of the E. coli DnaK substrate-binding domain in complex with pyrrhocoricin-derived peptide inhibitors. The structures show that pyrrhocoricins act as site-specific, dual-mode (competitive and allosteric) inhibitors, occupying the substrate-binding tunnel and disrupting the latch between the lid and the beta-sandwich. Our structural analysis revealed an allosteric coupling between the movements of the lid and the interdomain linker, identifying a previously unknown mechanism of the lid-mediated regulation of the chaperone cycle.

PubMed: 19103929
DOI: 10.1128/JB.01131-08

実験手法

X-RAY DIFFRACTION (2.6 Å)