2MJG
Solution Structure of C-terminal AbrB
Summary for 2MJG
| Entry DOI | 10.2210/pdb2mjg/pdb |
| NMR Information | BMRB: 18939 |
| Descriptor | Transition state regulatory protein AbrB (1 entity in total) |
| Functional Keywords | abrb, c-terminus, transcription |
| Biological source | Bacillus subtilis subsp. subtilis (Bacillus subtilis) |
| Total number of polymer chains | 2 |
| Total formula weight | 9993.43 |
| Authors | Olson, A.L.,Tucker, A.T.,Thompson, R.J.,Cavanagh, J. (deposition date: 2014-01-08, release date: 2014-11-26, Last modification date: 2024-05-01) |
| Primary citation | Olson, A.L.,Tucker, A.T.,Bobay, B.G.,Soderblom, E.J.,Moseley, M.A.,Thompson, R.J.,Cavanagh, J. Structure and DNA-binding traits of the transition state regulator AbrB. Structure, 22:1650-1656, 2014 Cited by PubMed Abstract: The AbrB protein from Bacillus subtilis is a DNA-binding global regulator controlling the onset of a vast array of protective functions under stressful conditions. Such functions include biofilm formation, antibiotic production, competence development, extracellular enzyme production, motility, and sporulation. AbrB orthologs are known in a variety of prokaryotic organisms, most notably in all infectious strains of Clostridia, Listeria, and Bacilli. Despite its central role in bacterial response and defense, its structure has been elusive because of its highly dynamic character. Orienting its N- and C-terminal domains with respect to one another has been especially problematic. Here, we have generated a structure of full-length, tetrameric AbrB using nuclear magnetic resonance, chemical crosslinking, and mass spectrometry. We note that AbrB possesses a strip of positive electrostatic potential encompassing its DNA-binding region and that its C-terminal domain aids in DNA binding. PubMed: 25308864DOI: 10.1016/j.str.2014.08.018 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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