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The outer-membrane export signal of Porphyromonas gingivalis type IX secretion system (T9SS) is a conserved C-terminal β-sandwich domain
- Source :
- 'Scientific Reports ', vol: 6, pages: 23123-1-23123-17 (2016), Scientific Reports, de Diego, I, Ksiazek, M, Mizgalska, D, Koneru, L, Golik, P, Szmigielski, B, Nowak, M, Nowakowska, Z, Potempa, B, Houston, J A, Enghild, J J, Thøgersen, I B, Gao, J, Kwan, A H, Trewhella, J, Dubin, G, Gomis-Rüth, F X, Nguyen, K-A & Potempa, J 2016, ' The outer-membrane export signal of Porphyromonas gingivalis type IX secretion system (T9SS) is a conserved C-terminal β-sandwich domain ', Scientific Reports, vol. 6, pp. 23123 . https://doi.org/10.1038/srep23123, Digital.CSIC. Repositorio Institucional del CSIC, instname
- Publication Year :
- 2016
- Publisher :
- Springer Science and Business Media LLC, 2016.
-
Abstract
- Iñaki de Diego et al.<br />In the recently characterized Type IX Secretion System (T9SS), the conserved C-terminal domain (CTD) in secreted proteins functions as an outer membrane translocation signal for export of virulence factors to the cell surface in the Gram-negative Bacteroidetes phylum. In the periodontal pathogen Porphyromonas gingivalis, the CTD is cleaved off by PorU sortase in a sequence-independent manner, and anionic lipopolysaccharide (A-LPS) is attached to many translocated proteins, thus anchoring them to the bacterial surface. Here, we solved the atomic structure of the CTD of gingipain B (RgpB) from P. gingivalis, alone and together with a preceding immunoglobulin-superfamily domain (IgSF). The CTD was found to possess a typical Ig-like fold encompassing seven antiparallel β-strands organized in two β-sheets, packed into a β-sandwich structure that can spontaneously dimerise through C-terminal strand swapping. Small angle X-ray scattering (SAXS) revealed no fixed orientation of the CTD with respect to the IgSF. By introducing insertion or substitution of residues within the inter-domain linker in the native protein, we were able to show that despite the region being unstructured, it nevertheless is resistant to general proteolysis. These data suggest structural motifs located in the two adjacent Ig-like domains dictate the processing of CTDs by the T9SS secretion pathway.<br />This study was financially supported in part by grants from European, US American, Polish, Spanish, and Catalan agencies (UMO-2012/04/A/NZ1/00051, UMO-2012/05/B/NZ6/00581, UMO-2013/08/W/NZ1/00696, UMO-2011/01/D/NZ1/01169, 2975/7.PR/13/2014/2, NIH NIDCR DE09761; FP7-PEOPLE-2011-ITN-290246 “RAPID”; FP7-HEALTH-2012-306029-2 “TRIGGER”; BFU2012-32862; BIO2013-49320-EXP; MDM-2014-0435; 1306/MOB/IV/2015/0 (“Mobilność Plus” MK) and 2014SGR9). The Department of Structural Biology of IBMB is a “María de Maeztu” Unit of Excellence from the Ministry of Economy and Competitiveness. Funding for data collection was provided in part by ESRF
- Subjects :
- Models, Molecular
0301 basic medicine
030106 microbiology
Immunoglobulins
Article
Protein Structure, Secondary
03 medical and health sciences
Bacterial Proteins
Sortase
Scattering, Small Angle
Secretion
Amino Acid Sequence
Structural motif
Bacterial Secretion Systems
Porphyromonas gingivalis
Conserved Sequence
Nuclear Export Signals
Genetics
Binding Sites
Multidisciplinary
biology
biology.organism_classification
3. Good health
Cell biology
Gingipain
Protein Transport
Secretory protein
CTD
Bacterial outer membrane
Subjects
Details
- ISSN :
- 20452322
- Volume :
- 6
- Database :
- OpenAIRE
- Journal :
- Scientific Reports
- Accession number :
- edsair.doi.dedup.....7f61a71d32523ea68b75321c70a5c229