3WKM

The periplasmic PDZ tandem fragment of the RseP homologue from Aquifex aeolicus in complex with the Fab fragment

Summary for 3WKM

• Entry DOI: 10.2210/pdb3wkm/pdb
• Related: 3WKL
• Descriptor: Putative zinc metalloprotease aq_1964, MOUSE IGG1-KAPPA FAB (HEAVY CHAIN), MOUSE IGG1-KAPPA FAB (LIGHT CHAIN), ... (4 entities in total)
• Functional Keywords: pdz domain, hydrolase
• Biological source: Aquifex aeolicus; More
• Cellular location: Cell inner membrane; Multi-pass membrane protein (By similarity): O67776
• Total number of polymer chains: 6
• Total formula weight: 136691.92

Authors

Nogi, T.,Tabata, S.,Tamura-kawakami, K.,Takagi, J. (deposition date: 2013-10-28, release date: 2013-12-18, Last modification date: 2024-10-09)

Primary citation

Hizukuri, Y.,Oda, T.,Tabata, S.,Tamura-kawakami, K.,Oi, R.,Sato, M.,Takagi, J.,Akiyama, Y.,Nogi, T.
A Structure-Based Model of Substrate Discrimination by a Noncanonical PDZ Tandem in the Intramembrane-Cleaving Protease RseP
Structure, 22:326-336, 2013

PubMed Abstract: During the extracytoplasmic stress response in Escherichia coli, the intramembrane protease RseP cleaves the anti-σ(E) protein RseA only after the membrane-anchored protease DegS truncates the periplasmic part of RseA that suppresses the action of RseP. Here we analyzed the three-dimensional structure of the two tandemly arranged PSD-95/Dlg/ZO-1 (PDZ) domains (PDZ tandem) present in the periplasmic region of RseP and revealed that the two putative ligand-binding grooves constitute a single pocket-like structure that would lie just above the active center sequestrated within the membrane. Complete removal of the PDZ tandem from RseP led to the intramembrane cleavage of RseA without prior truncation by DegS. Furthermore, mutations expected to destabilize the tertiary structure of the PDZ tandem also caused the deregulation of the sequential cleavage. These observations suggest that the PDZ tandem serves as a size-exclusion filter to accommodate the truncated form of RseA into the active center.

PubMed: 24389025
DOI: 10.1016/j.str.2013.12.003

Experimental method

X-RAY DIFFRACTION (2.2 Å)