4C2C
Crystal structure of the protease CtpB in an active state
Summary for 4C2C
| Entry DOI | 10.2210/pdb4c2c/pdb |
| Related | 4C2D 4C2E 4C2F 4C2G 4C2H |
| Descriptor | CARBOXY-TERMINAL PROCESSING PROTEASE CTPB, PEPTIDE1, PEPTIDE2, ... (4 entities in total) |
| Functional Keywords | hydrolase, pdz-proteases, allosteric regulation, conformational switch, sporulation, proteolytic tunnel |
| Biological source | BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168 More |
| Cellular location | Forespore intermembrane space: O35002 |
| Total number of polymer chains | 3 |
| Total formula weight | 50843.99 |
| Authors | Mastny, M.,Heuck, A.,Kurzbauer, R.,Clausen, T. (deposition date: 2013-08-17, release date: 2013-12-04, Last modification date: 2024-10-16) |
| Primary citation | Mastny, M.,Heuck, A.,Kurzbauer, R.,Heiduk, A.,Boisguerin, P.,Volkmer, R.,Ehrmann, M.,Rodrigues, C.D.A.,Rudner, D.Z.,Clausen, T. Ctpb Assembles a Gated Protease Tunnel Regulating Cell-Cell Signaling During Spore Formation in Bacillus Subtilis. Cell(Cambridge,Mass.), 155:647-, 2013 Cited by PubMed Abstract: 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. PubMed: 24243021DOI: 10.1016/J.CELL.2013.09.050 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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