8RQY
MakC and MakD are two proteins associated with a tripartite toxin of Vibrio cholerae
Summary for 8RQY
| Entry DOI | 10.2210/pdb8rqy/pdb |
| Descriptor | Inclusion body protein (2 entities in total) |
| Functional Keywords | vibrio mak operon encoded protein, toxin associated protein unknown function, unknown function |
| Biological source | Vibrio cholerae O1 biovar El Tor str. N16961 |
| Total number of polymer chains | 1 |
| Total formula weight | 14529.37 |
| Authors | Bodra, N.,Persson, K.,Nadeem, A.,Wai, S.N.,Toh, E. (deposition date: 2024-01-21, release date: 2024-09-25, Last modification date: 2024-10-30) |
| Primary citation | Bodra, N.,Toh, E.,Nadeem, A.,Wai, S.N.,Persson, K. MakC and MakD are two proteins associated with a tripartite toxin of Vibrio cholerae . Front Microbiol, 15:1457850-1457850, 2024 Cited by PubMed Abstract: Pathogenic serotypes of , transmitted through contaminated water and food, are responsible for outbreaks of cholera, an acute diarrheal disease. While the cholera toxin is the primary virulence factor, also expresses other virulence factors, such as the tripartite toxin MakABE that is secreted via the bacterial flagellum. These three proteins are co-expressed with two accessory proteins, MakC and MakD, whose functions remain unknown. Here, we present the crystal structures of MakC and MakD, revealing that they are similar in both sequence and structure but lack other close structural relatives. Our study further investigates the roles of MakC and MakD, focusing on their impact on the expression and secretion of the components of the MakABE tripartite toxin. Through deletion mutant analysis, we found that individual deletions of or do not significantly affect MakA expression or secretion. However, the deletion of both and impairs the expression of MakB, which is directly downstream, and decreases the expression of MakE, which is separated from by two genes. Conversely, MakA, encoded by the gene located between and is expressed normally but its secretion is impaired. Additionally, our findings indicate that MakC, in contrast to MakD, exhibits strong interactions with other proteins. Furthermore, both MakC and MakD were observed to be localized within the cytosol of the bacterial cell. This study provides new insights into the regulatory mechanisms affecting the Mak protein family in and highlights the complex interplay between gene proximity and protein expression. PubMed: 39421563DOI: 10.3389/fmicb.2024.1457850 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.045 Å) |
Structure validation
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