4C2H

Crystal structure of the CtpB(V118Y) mutant

4C2H の概要

• エントリーDOI: 10.2210/pdb4c2h/pdb
• 関連するPDBエントリー: 4C2C 4C2D 4C2E 4C2F 4C2G
• 分子名称: CARBOXY-TERMINAL PROCESSING PROTEASE CTPB (2 entities in total)
• 機能のキーワード: hydrolase, pdz-proteases, allosteric regulation, conformational switch, sporulation, proteolytic tunnel
• 由来する生物種: BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168
• 細胞内の位置: Forespore intermembrane space: O35002
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 99697.16

構造登録者

Mastny, M.,Heuck, A.,Kurzbauer, R.,Clausen, T. (登録日: 2013-08-17, 公開日: 2013-12-04, 最終更新日: 2023-12-20)

主引用文献

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

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: 24243021
DOI: 10.1016/J.CELL.2013.09.050

実験手法

X-RAY DIFFRACTION (1.95 Å)