3ID3

Crystal Structure of RseP PDZ2 I304A domain

Summary for 3ID3

• Entry DOI: 10.2210/pdb3id3/pdb
• Related: 3ID1 3ID2 3ID4
• Descriptor: Regulator of sigma E protease (2 entities in total)
• Functional Keywords: hydrolase, cell inner membrane, cell membrane, membrane, metal-binding, metalloprotease, protease, transmembrane, zinc
• Biological source: Escherichia coli K-12
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P0AEH1
• Total number of polymer chains: 2
• Total formula weight: 18855.75

Authors

Li, X.,Wang, B.,Feng, L.,Wang, J.,Shi, Y. (deposition date: 2009-07-20, release date: 2009-08-11, Last modification date: 2023-11-01)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.01 Å)