8HER

Solution structure of the periplasmic domain of RsgI6 from Clostridium thermocellum

8HER の概要

• エントリーDOI: 10.2210/pdb8her/pdb
• 関連するPDBエントリー: 6IVS 6IVU 8HDJ 8HEP 8HEQ
• NMR情報: BMRB: 36516
• 分子名称: Anti-sigma factor (2 entities in total)
• 機能のキーワード: anti-sigma factor; transcription, signaling protein
• 由来する生物種: Acetivibrio thermocellus DSM 1313; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19818.33

構造登録者

Chen, C.,Feng, Y. (登録日: 2022-11-08, 公開日: 2023-05-24, 最終更新日: 2024-05-15)

主引用文献

Chen, C.,Dong, S.,Yu, Z.,Qiao, Y.,Li, J.,Ding, X.,Li, R.,Lin, J.,Bayer, E.A.,Liu, Y.J.,Cui, Q.,Feng, Y.
Essential autoproteolysis of bacterial anti-sigma factor RsgI for transmembrane signal transduction.
Sci Adv, 9:eadg4846-eadg4846, 2023

PubMed Abstract: Autoproteolysis has been discovered to play key roles in various biological processes, but functional autoproteolysis has been rarely reported for transmembrane signaling in prokaryotes. In this study, an autoproteolytic effect was discovered in the conserved periplasmic domain of anti-σ factor RsgIs from , which was found to transmit extracellular polysaccharide-sensing signals into cells for regulation of the cellulosome system, a polysaccharide-degrading multienzyme complex. Crystal and NMR structures of periplasmic domains from three RsgIs demonstrated that they are different from all known proteins that undergo autoproteolysis. The RsgI-based autocleavage site was located at a conserved Asn-Pro motif between the β1 and β2 strands in the periplasmic domain. This cleavage was demonstrated to be essential for subsequent regulated intramembrane proteolysis to activate the cognate SigI, in a manner similar to that of autoproteolysis-dependent activation of eukaryotic adhesion G protein-coupled receptors. These results indicate the presence of a unique prevalent type of autoproteolytic phenomenon in bacteria for signal transduction.

PubMed: 37418529
DOI: 10.1126/sciadv.adg4846

実験手法

SOLUTION NMR