3GBG
Crystal Structure of ToxT from Vibrio Cholerae O395
Summary for 3GBG
| Entry DOI | 10.2210/pdb3gbg/pdb |
| Descriptor | TCP pilus virulence regulatory protein, PALMITOLEIC ACID (3 entities in total) |
| Functional Keywords | cupin, helix-turn-helix, arac family, activator, dna-binding, transcription, transcription regulation, virulence, transcription regulator |
| Biological source | Vibrio cholerae |
| Cellular location | Cytoplasm (By similarity): A5F384 |
| Total number of polymer chains | 1 |
| Total formula weight | 32346.43 |
| Authors | Lowden, M.J.,Kull, F.J. (deposition date: 2009-02-19, release date: 2010-02-23, Last modification date: 2024-04-03) |
| Primary citation | Lowden, M.J.,Skorupski, K.,Pellegrini, M.,Chiorazzo, M.G.,Taylor, R.K.,Kull, F.J. Structure of Vibrio cholerae ToxT reveals a mechanism for fatty acid regulation of virulence genes. Proc.Natl.Acad.Sci.USA, 107:2860-2865, 2010 Cited by PubMed Abstract: Cholera is an acute intestinal infection caused by the bacterium Vibrio cholerae. In order for V. cholerae to cause disease, it must produce two virulence factors, the toxin-coregulated pilus (TCP) and cholera toxin (CT), whose expression is controlled by a transcriptional cascade culminating with the expression of the AraC-family regulator, ToxT. We have solved the 1.9 A resolution crystal structure of ToxT, which reveals folds in the N- and C-terminal domains that share a number of features in common with AraC, MarA, and Rob as well as the unexpected presence of a buried 16-carbon fatty acid, cis-palmitoleate. The finding that cis-palmitoleic acid reduces TCP and CT expression in V. cholerae and prevents ToxT from binding to DNA in vitro provides a direct link between the host environment of V. cholerae and regulation of virulence gene expression. PubMed: 20133655DOI: 10.1073/pnas.0915021107 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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