8HDJ
Periplasmic domain of RsgI2 of Clostridium thermocellum
Summary for 8HDJ
| Entry DOI | 10.2210/pdb8hdj/pdb |
| Related | 6IVS 6IVU 8HEP 8HEQ 8HER |
| Descriptor | Periplasmic domain of RsgI2, Anti-sigma-I factor RsgI2 (3 entities in total) |
| Functional Keywords | anti-sigmai, signaling protein |
| Biological source | Acetivibrio thermocellus DSM 1313 More |
| Total number of polymer chains | 8 |
| Total formula weight | 76570.10 |
| Authors | Chen, C.,Dong, S.,Feng, Y.G. (deposition date: 2022-11-04, release date: 2023-05-17, Last modification date: 2024-04-03) |
| Primary citation | 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 Cited by 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: 37418529DOI: 10.1126/sciadv.adg4846 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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