3OU0

re-refined 3CS0

3OU0 の概要

• エントリーDOI: 10.2210/pdb3ou0/pdb
• 関連するPDBエントリー: 3OTP
• 分子名称: Periplasmic serine endoprotease DegP, pentapeptide, heptapeptide (3 entities in total)
• 機能のキーワード: protease, hydrolase
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side: P0C0V0
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 48566.74

構造登録者

Sauer, R.T.,Grant, R.A.,Kim, S. (登録日: 2010-09-14, 公開日: 2011-01-19, 最終更新日: 2024-11-06)

主引用文献

Kim, S.,Grant, R.A.,Sauer, R.T.
Covalent Linkage of Distinct Substrate Degrons Controls Assembly and Disassembly of DegP Proteolytic Cages.
Cell(Cambridge,Mass.), 145:67-78, 2011

PubMed Abstract: Protein quality control requires careful regulation of intracellular proteolysis. For DegP, a periplasmic protease, substrates promote assembly of inactive hexamers into proteolytically active cages with 12, 18, 24, or 30 subunits. Here, we show that sensitive activation and cage assembly require covalent linkage of distinct substrate sequences that affect degradation (degrons). One degron binds the DegP active site, and another degron binds a separate tethering site in PDZ1 in the crystal structure of a substrate-bound DegP dodecamer. FRET experiments demonstrate that active cages assemble rapidly in a reaction that is positively cooperative in substrate concentration, remain stably assembled while uncleaved substrate is present, and dissociate once degradation is complete. Thus, the energy of binding of linked substrate degrons drives assembly of the proteolytic machine responsible for subsequent degradation. Substrate cleavage and depletion results in disassembly, ensuring that DegP is proteolytically active only when sufficient quantities of protein substrates are present.

PubMed: 21458668
DOI: 10.1016/j.cell.2011.02.024

実験手法

X-RAY DIFFRACTION (3 Å)