1KY9

Crystal Structure of DegP (HtrA)

1KY9 の概要

• エントリーDOI: 10.2210/pdb1ky9/pdb
• 分子名称: PROTEASE DO (2 entities in total)
• 機能のキーワード: protein quality control, serine protease, trypsin, chaperone, pdz, atp-independent, temperature-regulated, periplasm, cage-forming protein, hydrolase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm: P0C0V0
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 95018.90

構造登録者

Krojer, T.,Garrido-Franco, M.,Huber, R.,Ehrmann, M.,Clausen, T. (登録日: 2002-02-04, 公開日: 2002-04-03, 最終更新日: 2024-11-13)

主引用文献

Krojer, T.,Garrido-Franco, M.,Huber, R.,Ehrmann, M.,Clausen, T.
Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine.
Nature, 416:455-459, 2002

PubMed Abstract: Molecular chaperones and proteases monitor the folded state of other proteins. In addition to recognizing non-native conformations, these quality control factors distinguish substrates that can be refolded from those that need to be degraded. To investigate the molecular basis of this process, we have solved the crystal structure of DegP (also known as HtrA), a widely conserved heat shock protein that combines refolding and proteolytic activities. The DegP hexamer is formed by staggered association of trimeric rings. The proteolytic sites are located in a central cavity that is only accessible laterally. The mobile side-walls are constructed by twelve PDZ domains, which mediate the opening and closing of the particle and probably the initial binding of substrate. The inner cavity is lined by several hydrophobic patches that may act as docking sites for unfolded polypeptides. In the chaperone conformation, the protease domain of DegP exists in an inactive state, in which substrate binding in addition to catalysis is abolished.

PubMed: 11919638
DOI: 10.1038/416455a

実験手法

X-RAY DIFFRACTION (2.8 Å)