3wkm

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

spinqualitylabelsall models 3wkm, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3wkm is a 6 chain structure with sequence from Aquifex aeolicus VF5 and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Y1964_AQUAE Publication Abstract from PubMed During the extracytoplasmic stress response in Escherichia coli, the intramembrane protease RseP cleaves the anti-sigma(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. A Structure-Based Model of Substrate Discrimination by a Noncanonical PDZ Tandem in the Intramembrane-Cleaving Protease RseP.,Hizukuri Y, Oda T, Tabata S, Tamura-Kawakami K, Oi R, Sato M, Takagi J, Akiyama Y, Nogi T Structure. 2014 Feb 4;22(2):326-36. doi: 10.1016/j.str.2013.12.003. Epub 2014 Jan, 2. PMID:24389025 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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