2K9S
Solution structure of dna binding domain of E. coli arac
Summary for 2K9S
| Entry DOI | 10.2210/pdb2k9s/pdb |
| Related | 1BL0 1D5Y 1XJA 2AAC 2ARA 2ARC |
| NMR Information | BMRB: 16001 |
| Descriptor | Arabinose operon regulatory protein (1 entity in total) |
| Functional Keywords | activator, arabinose catabolism, carbohydrate metabolism, cytoplasm, dna-binding, repressor, transcription, transcription regulation |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 12096.71 |
| Authors | Rodgers, M.E.,Schleif, R.F. (deposition date: 2008-10-23, release date: 2008-11-25, Last modification date: 2024-05-08) |
| Primary citation | Rodgers, M.E.,Schleif, R. Solution structure of the DNA binding domain of AraC protein. Proteins, 77:202-208, 2009 Cited by PubMed Abstract: We report the solution structure of the DNA binding domain of the Escherichia coli regulatory protein AraC determined in the absence of DNA. The 20 lowest energy structures, determined on the basis of 1507 unambiguous nuclear Overhauser restraints and 180 angle restraints, are well resolved with a pair wise backbone root mean square deviation of 0.7 A. The protein, free of DNA, is well folded in solution and contains seven helices arranged in two semi-independent sub domains, each containing one helix-turn-helix DNA binding motif, joined by a 19 residue central helix. This solution structure is discussed in the context of extensive biochemical and physiological data on AraC and with respect to the DNA-bound structures of the MarA and Rob homologs. PubMed: 19422057DOI: 10.1002/prot.22431 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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