1P4W
Solution structure of the DNA-binding domain of the Erwinia amylovora RcsB protein
Summary for 1P4W
| Entry DOI | 10.2210/pdb1p4w/pdb |
| Descriptor | rcsB (1 entity in total) |
| Functional Keywords | rcsb protein, solution structure, dna binding domain, dna binding protein |
| Biological source | Erwinia amylovora |
| Total number of polymer chains | 1 |
| Total formula weight | 10969.68 |
| Authors | Pristovsek, P.,Sengupta, K.,Loehr, F.,Schaefer, B.,Wehland von Trebra, M.,Rueterjans, H.,Bernhard, F. (deposition date: 2003-04-24, release date: 2003-06-17, Last modification date: 2024-05-22) |
| Primary citation | Pristovsek, P.,Sengupta, K.,Lohr, F.,Schafer, B.,von Trebra, M.W.,Ruterjans, H.,Bernhard, F. Structural analysis of the DNA-binding domain of the Erwinia amylovora RcsB protein and its interaction with the RcsAB box. J.Biol.Chem., 278:17752-17759, 2003 Cited by PubMed Abstract: The transcriptional regulator RcsB interacts with other coactivators to control the expression of biosynthetic operons in enterobacteria. While in a heterodimer complex with the regulator RcsA the RcsAB box consensus is recognized, DNA binding sites for RcsB without RcsA have also been identified. The conformation of RcsB might therefore be modulated upon interaction with various coactivators, resulting in the recognition of different DNA targets. We report the solution structure of the C-terminal DNA-binding domain of the RcsB protein from Erwinia amylovora spanning amino acid residues 129-215 solved by heteronuclear magnetic resonance (NMR) spectroscopy. The C-terminal domain is composed of four alpha-helices where two central helices form a helix-turn-helix motif similar to the structures of the regulatory proteins GerE, NarL, and TraR. Amino acid residues involved in the RcsA independent DNA binding of RcsB were identified by titration studies with a RcsAB box consensus fragment. Data obtained from NMR spectroscopy together with surface plasmon resonance measurements demonstrate that the RcsAB box is specifically recognized by the RcsAB heterodimer as well as by RcsB alone. However, the binding constant of RcsB alone at target promoters from Escherichia coli, E. amylovora, and Pantoea stewartii was approximately 1 order of magnitude higher compared with that of the RcsAB heterodimer. We present evidence that the obvious role of RcsA is not to alter the DNA binding specificity of RcsB but to stabilize RcsB-DNA complexes. PubMed: 12740396DOI: 10.1074/jbc.M301328200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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