3ID2

Crystal Structure of RseP PDZ2 domain

3ID2 の概要

• エントリーDOI: 10.2210/pdb3id2/pdb
• 関連するPDBエントリー: 3ID1 3ID3 3ID4
• 分子名称: Regulator of sigma E protease, IODIDE ION (2 entities in total)
• 機能のキーワード: hydrolase, cell inner membrane, cell membrane, membrane, metal-binding, metalloprotease, protease, transmembrane, zinc
• 由来する生物種: Escherichia coli K-12
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P0AEH1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 20485.25

構造登録者

Li, X.,Wang, B.,Feng, L.,Wang, J.,Shi, Y. (登録日: 2009-07-20, 公開日: 2009-08-11, 最終更新日: 2023-11-01)

主引用文献

Li, X.,Wang, B.,Feng, L.,Kang, H.,Qi, Y.,Wang, J.,Shi, Y.
Cleavage of RseA by RseP requires a carboxyl-terminal hydrophobic amino acid following DegS cleavage
Proc.Natl.Acad.Sci.USA, 106:14837-14842, 2009

PubMed Abstract: Regulated intramembrane proteolysis (RIP) by the Site-2 protease (S2P) results in the release of a transmembrane signaling protein. Curiously, however, S2P cleavage must be preceded by the action of the Site-1 protease (S1P). To decipher the underlying mechanism, we reconstituted sequential, in vitro cleavages of the Escherichia coli transmembrane protein RseA by DegS (S1P) and RseP (S2P). After DegS cleavage, the newly exposed carboxyl-terminal residue Val-148 of RseA plays an essential role for RseP cleavage, and its mutation to charged or dissimilar amino acids crippled the Site-2 cleavage. By contrast, the identity of residues 146 and 147 of RseA has no impact on Site-2 cleavage. These results explain why Site-1 cleavage must precede Site-2 cleavage. Structural analysis reveals that the putative peptide-binding groove in the second, but not the first, PDZ domain of RseP is poised for binding to a single hydrophobic amino acid. These observations suggest that after DegS cleavage, the newly exposed carboxyl terminus of RseA may facilitate Site-2 cleavage through direct interaction with the PDZ domain.

PubMed: 19706448
DOI: 10.1073/pnas.0903289106

実験手法

X-RAY DIFFRACTION (3.089 Å)