3KLN
Vibrio cholerae VpsT
Summary for 3KLN
| Entry DOI | 10.2210/pdb3kln/pdb |
| Related | 3KLO |
| Descriptor | Transcriptional regulator, LuxR family (1 entity in total) |
| Functional Keywords | rec domain, hth domain, dna-binding, transcription, transcription regulation |
| Biological source | Vibrio cholerae |
| Total number of polymer chains | 4 |
| Total formula weight | 103872.01 |
| Authors | Krasteva, P.V.,Navarro, V.A.S.,Sondermann, H. (deposition date: 2009-11-08, release date: 2010-02-09, Last modification date: 2024-02-21) |
| Primary citation | Krasteva, P.V.,Fong, J.C.,Shikuma, N.J.,Beyhan, S.,Navarro, M.V.,Yildiz, F.H.,Sondermann, H. Vibrio cholerae VpsT Regulates Matrix Production and Motility by Directly Sensing Cyclic di-GMP. Science, 327:866-868, 2010 Cited by PubMed Abstract: Microorganisms can switch from a planktonic, free-swimming life-style to a sessile, colonial state, called a biofilm, which confers resistance to environmental stress. Conversion between the motile and biofilm life-styles has been attributed to increased levels of the prokaryotic second messenger cyclic di-guanosine monophosphate (c-di-GMP), yet the signaling mechanisms mediating such a global switch are poorly understood. Here we show that the transcriptional regulator VpsT from Vibrio cholerae directly senses c-di-GMP to inversely control extracellular matrix production and motility, which identifies VpsT as a master regulator for biofilm formation. Rather than being regulated by phosphorylation, VpsT undergoes a change in oligomerization on c-di-GMP binding. PubMed: 20150502DOI: 10.1126/science.1181185 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.078 Å) |
Structure validation
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