4c2f

Crystal structure of the CtpB R168A mutant present in an active conformation

spinqualitylabelsall models 4c2f, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4c2f is a 3 chain structure with sequence from Bacsu and Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: MSE Related: 4c2c, 4c2d, 4c2e, 4c2g, 4c2h Activity: C-terminal processing peptidase, with EC number 3.4.21.102 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CTPB_BACSU] Involved in the signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro-sigma-K during sporulation. The signaling serine protease CtpB triggers pro-sigma-K processing by cleaving the regulatory protein SpoIVFA and is necessary for the proper timing of sigma-K activation. Publication Abstract from PubMed Spore formation in Bacillus subtilis relies on a regulated intramembrane proteolysis (RIP) pathway that synchronizes mother-cell and forespore development. To address the molecular basis of this SpoIV transmembrane signaling, we carried out a structure-function analysis of the activating protease CtpB. Crystal structures reflecting distinct functional states show that CtpB constitutes a ring-like protein scaffold penetrated by two narrow tunnels. Access to the proteolytic sites sequestered within these tunnels is controlled by PDZ domains that rearrange upon substrate binding. Accordingly, CtpB resembles a minimal version of a self-compartmentalizing protease regulated by a unique allosteric mechanism. Moreover, biochemical analysis of the PDZ-gated channel combined with sporulation assays reveal that activation of the SpoIV RIP pathway is induced by the concerted activity of CtpB and a second signaling protease, SpoIVB. This proteolytic mechanism is of broad relevance for cell-cell communication, illustrating how distinct signaling pathways can be integrated into a single RIP module. CtpB Assembles a Gated Protease Tunnel Regulating Cell-Cell Signaling during Spore Formation in Bacillus subtilis.,Mastny M, Heuck A, Kurzbauer R, Heiduk A, Boisguerin P, Volkmer R, Ehrmann M, Rodrigues CD, Rudner DZ, Clausen T Cell. 2013 Oct 24;155(3):647-58. doi: 10.1016/j.cell.2013.09.050. Epub 2013 Oct, 24. PMID:24243021 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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