5Y1A
HBP35 of Porphyromonas gingivalis
Summary for 5Y1A
Entry DOI | 10.2210/pdb5y1a/pdb |
Descriptor | 35 kDa hemin binding protein (2 entities in total) |
Functional Keywords | porphyromonas gingivalis, beta-sandwich domain, thioredoxin domain, electron transport |
Biological source | Porphyromonas gingivalis |
Total number of polymer chains | 1 |
Total formula weight | 37605.39 |
Authors | Kakuda, S.,Suzuki, M.,Sato, K. (deposition date: 2017-07-20, release date: 2018-07-25, Last modification date: 2024-03-27) |
Primary citation | Sato, K.,Kakuda, S.,Yukitake, H.,Kondo, Y.,Shoji, M.,Takebe, K.,Narita, Y.,Naito, M.,Nakane, D.,Abiko, Y.,Hiratsuka, K.,Suzuki, M.,Nakayama, K. Immunoglobulin-like domains of the cargo proteins are essential for protein stability during secretion by the type IX secretion system. Mol. Microbiol., 110:64-81, 2018 Cited by PubMed Abstract: The periodontal pathogen Porphyromonas gingivalis secretes many potent virulence factors using the type IX secretion system (T9SS). T9SS cargo proteins that have been structurally determined by X-ray crystallography are composed of a signal peptide, functional domain(s), an immunoglobulin (Ig)-like domain and a C-terminal domain. Role of the Ig-like domains of cargo proteins in the T9SS has not been elucidated. Gingipain proteases, which are cargo proteins of the T9SS, were degraded when their Ig-like domains were lacking or truncated. The degradation was dependent on the activity of a quality control factor, HtrA protease. Another T9SS cargo protein, HBP35, which has a thioredoxin domain as a functional domain, was analyzed by X-ray crystallography, revealing that HBP35 has an Ig-like domain after the thioredoxin domain and that the hydrophobic regions of the thioredoxin domain and the Ig-like domain face each other. HBP35 with substitution of hydrophobic amino acids in the Ig-like domain was degraded depending on HtrA. These results suggest that the Ig-like domain mediates stability of the cargo proteins in the T9SS. PubMed: 30030863DOI: 10.1111/mmi.14083 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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