2FY9
Solution Structure of the N-Terminal DNA Recognition Domain of the Bacillus Subtilis Transcription-State Regulator ABH
Summary for 2FY9
| Entry DOI | 10.2210/pdb2fy9/pdb |
| Related | 1YSF 1Z0R |
| NMR Information | BMRB: 6826 |
| Descriptor | Putative transition state regulator abh (1 entity in total) |
| Functional Keywords | n-terminal dna-binding domain, transition state regulator, transcription |
| Biological source | Bacillus subtilis |
| Total number of polymer chains | 2 |
| Total formula weight | 12332.91 |
| Authors | Cavanagh, J.,Bobay, B.G. (deposition date: 2006-02-07, release date: 2006-05-23, Last modification date: 2024-05-29) |
| Primary citation | Bobay, B.G.,Mueller, G.A.,Thompson, R.J.,Murzin, A.G.,Venters, R.A.,Strauch, M.A.,Cavanagh, J. NMR Structure of AbhN and Comparison with AbrBN: First insights into the DNA-binding promiscuity and specificity of AbrB-like transition-state regulator proteins J.Biol.Chem., 281:21399-21409, 2006 Cited by PubMed Abstract: Understanding the molecular mechanisms of transition state regulator proteins is critical, since they play a pivotal role in the ability of bacteria to cope with changing environments. Although much effort has focused on their genetic characterization, little is known about their structural and functional conservation. Here we present the high resolution NMR solution structure of the N-terminal domain of the Bacillus subtilis transition state regulator Abh (AbhN), only the second such structure to date. We then compare AbhN to the N-terminal DNA-binding domain of B. subtilis AbrB (AbrBN). This is the first such comparison between two AbrB-like transition state regulators. AbhN and AbrBN are very similar, suggesting a common structural basis for their DNA binding. However, we also note subtle variances between the AbhN and AbrBN structures, which may play important roles in DNA target specificity. The results of accompanying in vitro DNA-binding studies serve to highlight binding differences between the two proteins. PubMed: 16702211DOI: 10.1074/jbc.M601963200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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