4A8D

DegP dodecamer with bound OMP

4A8D の概要

• エントリーDOI: 10.2210/pdb4a8d/pdb
• 関連するPDBエントリー: 1KY9 2J1N 2J4U
• EMDBエントリー: 1505
• 分子名称: PERIPLASMIC SERINE ENDOPROTEASE DEGP, OUTER MEMBRANE PROTEIN C (2 entities in total)
• 機能のキーワード: hydrolase-transport protein complex, chaperone, hydrolase/transport protein
• 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; Cell outer membrane; Multi-pass membrane protein: P06996
• タンパク質・核酸の鎖数: 13
• 化学式量合計: 600571.35

構造登録者

Malet, H.,Krojer, T.,Sawa, J.,Schafer, E.,Saibil, H.R.,Ehrmann, M.,Clausen, T. (登録日: 2011-11-20, 公開日: 2012-01-11, 最終更新日: 2024-05-08)

主引用文献

Malet, H.,Canellas, F.,Sawa, J.,Yan, J.,Thalassinos, K.,Ehrmann, M.,Clausen, T.,Saibil, H.R.
Newly Folded Substrates Inside the Molecular Cage of the Htra Chaperone Degq
Nat.Struct.Mol.Biol., 19:152-, 2012

PubMed Abstract: The HtrA protein family combines chaperone and protease activities and is essential for protein quality control in many organisms. Whereas the mechanisms underlying the proteolytic function of HtrA proteins are well characterized, their chaperone activity remains poorly understood. Here we describe cryo-EM structures of Escherichia coli DegQ in its 12- and 24-mer states in complex with model substrates, providing a structural model of HtrA chaperone action. Up to six lysozyme substrates bind inside the DegQ 12-mer cage and are visualized in a close-to-native state. An asymmetric reconstruction reveals the binding of a well-ordered lysozyme to four DegQ protomers. DegQ PDZ domains are located adjacent to substrate density and their presence is required for chaperone activity. The substrate-interacting regions appear conserved in 12- and 24-mer cages, suggesting a common mechanism of chaperone function.

PubMed: 22245966
DOI: 10.1038/NSMB.2210

実験手法

ELECTRON MICROSCOPY (28 Å)