5NFI
The fimbrial anchor protein Mfa2 from Porphyromonas gingivalis
Summary for 5NFI
| Entry DOI | 10.2210/pdb5nfi/pdb |
| Descriptor | Minor fimbrium anchoring subunit Mfa2, IODIDE ION (3 entities in total) |
| Functional Keywords | fimbria, adhesin, periodontitis, cell adhesion |
| Biological source | Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) |
| Cellular location | Cell outer membrane ; Lipid-anchor : B2RHG2 |
| Total number of polymer chains | 1 |
| Total formula weight | 32207.13 |
| Authors | Hall, M.,Hasegawa, Y.,Persson, K.,Yoshimura, F. (deposition date: 2017-03-14, release date: 2018-02-07, Last modification date: 2024-11-20) |
| Primary citation | Hall, M.,Hasegawa, Y.,Yoshimura, F.,Persson, K. Structural and functional characterization of shaft, anchor, and tip proteins of the Mfa1 fimbria from the periodontal pathogen Porphyromonas gingivalis. Sci Rep, 8:1793-1793, 2018 Cited by PubMed Abstract: Very little is known about how fimbriae of Bacteroidetes bacteria are assembled. To shed more light on this process, we solved the crystal structures of the shaft protein Mfa1, the regulatory protein Mfa2, and the tip protein Mfa3 from the periodontal pathogen Porphyromonas gingivalis. Together these build up part of the Mfa1 fimbria and represent three of the five proteins, Mfa1-5, encoded by the mfa1 gene cluster. Mfa1, Mfa2 and Mfa3 have the same overall fold i.e., two β-sandwich domains. Upon polymerization, the first β-strand of the shaft or tip protein is removed by indigenous proteases. Although the resulting void is expected to be filled by a donor-strand from another fimbrial protein, the mechanism by which it does so is still not established. In contrast, the first β-strand in Mfa2, the anchoring protein, is firmly attached by a disulphide bond and is not cleaved. Based on the structural information, we created multiple mutations in P. gingivalis and analysed their effect on fimbrial polymerization and assembly in vivo. Collectively, these data suggest an important role for the C-terminal tail of Mfa1, but not of Mfa3, affecting both polymerization and maturation of downstream fimbrial proteins. PubMed: 29379120DOI: 10.1038/s41598-018-20067-z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.508 Å) |
Structure validation
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