6ovk

Crystal Structure of the Pseudomonas capeferrum Anti-sigma Regulator PupR C-terminal Cell-surface Signaling Domain in Complex with the Outer Membrane Transporter PupB N-terminal Signaling Domain

spinqualitylabelsall models 6ovk, resolution 1.76Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ovk is a 2 chain structure with sequence from Pseudomonas capeferrum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.761Å Ligands: TLA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Cell-surface signaling (CSS) in Gram-negative bacteria involves highly conserved regulatory pathways that optimize gene expression by transducing extracellular environmental signals to the cytoplasm via inner-membrane sigma regulators. The molecular details of ferric siderophore-mediated activation of the iron import machinery through a sigma regulator are unclear. Here, we present the 1.56 A resolution structure of the periplasmic complex of the C-terminal CSS domain (CCSSD) of PupR, the sigma regulator in the Pseudomonas capeferrum pseudobactin BN7/8 transport system, and the N-terminal signaling domain (NTSD) of PupB, an outer-membrane TonB-dependent transducer. The structure revealed that the CCSSD consists of two subdomains: a juxta-membrane subdomain, which has a novel all-beta fold, followed by a secretin/TonB, short N-terminal subdomain at the C-terminus of the CCSSD, a previously unobserved topological arrangement of this domain. Using affinity pull-down assays, isothermal titration calorimetry, and thermal denaturation circular dichroism spectroscopy; we show that both subdomains are required for binding the NTSD with micromolar affinity and that NTSD binding improves CCSSD stability. Our findings prompt us to present a revised model of CSS wherein the CCSSD:NTSD complex forms prior to ferric-siderophore binding. Upon siderophore binding, conformational changes in the CCSSD enable regulated intramembrane proteolysis of the sigma regulator, ultimately resulting in transcriptional regulation. Structural basis of cell surface signaling by a conserved sigma regulator in Gram-negative bacteria.,Jensen JL, Jernberg BD, Sinha S, Colbert CL J Biol Chem. 2020 Feb 26. pii: RA119.010697. doi: 10.1074/jbc.RA119.010697. PMID:32107313 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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