5TN0
Solution Structure of the N-terminal DNA-binding domain of the master biofilm-regulator SinR from Bacillus subtilis
Summary for 5TN0
| Entry DOI | 10.2210/pdb5tn0/pdb |
| Related | 5TMX 5TN2 |
| NMR Information | BMRB: 30193 |
| Descriptor | HTH-type transcriptional regulator SinR (1 entity in total) |
| Functional Keywords | biofilm formation, transcription |
| Biological source | Bacillus subtilis (strain 168) |
| Total number of polymer chains | 1 |
| Total formula weight | 7847.91 |
| Authors | Draughn, G.L.,Bobay, B.G.,Stowe, S.D.,Thompson, R.J.,Cavanagh, J. (deposition date: 2016-10-13, release date: 2017-10-25, Last modification date: 2024-05-01) |
| Primary citation | Milton, M.E.,Draughn, G.L.,Bobay, B.G.,Stowe, S.D.,Olson, A.L.,Feldmann, E.A.,Thompson, R.J.,Myers, K.H.,Santoro, M.T.,Kearns, D.B.,Cavanagh, J. The Solution Structures and Interaction of SinR and SinI: Elucidating the Mechanism of Action of the Master Regulator Switch for Biofilm Formation in Bacillus subtilis. J.Mol.Biol., 2019 Cited by PubMed Abstract: Bacteria have developed numerous protection strategies to ensure survival in harsh environments, with perhaps the most robust method being the formation of a protective biofilm. In biofilms, bacterial cells are embedded within a matrix that is composed of a complex mixture of polysaccharides, proteins, and DNA. The gram-positive bacterium Bacillus subtilis has become a model organism for studying regulatory networks directing biofilm formation. The phenotypic transition from a planktonic to biofilm state is regulated by the activity of the transcriptional repressor, SinR, and its inactivation by its primary antagonist, SinI. In this work, we present the first full-length structural model of tetrameric SinR using a hybrid approach combining high-resolution solution nuclear magnetic resonance (NMR), chemical cross-linking, mass spectrometry, and molecular docking. We also present the solution NMR structure of the antagonist SinI dimer and probe the mechanism behind the SinR-SinI interaction using a combination of biochemical and biophysical techniques. As a result of these findings, we propose that SinI utilizes a residue replacement mechanism to block SinR multimerization, resulting in diminished DNA binding and concomitant decreased repressor activity. Finally, we provide an evidence-based mechanism that confirms how disruption of the SinR tetramer by SinI regulates gene expression. PubMed: 31493408DOI: 10.1016/j.jmb.2019.08.019 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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