title: NMR structure of AbhN and comparison with AbrBN: FIRST insights into the DNA binding promiscuity and specificity of AbrB-like transition state regulator proteins.
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.
authors.affiliation: Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina 27695.
authors.forename: Benjamin G
authors.initials: BG
authors.lastname: Bobay
authors.affiliation: Laboratory of Structural Biology, NIEHS, National Institutes of Health, Research Triangle Park, North Carolina 27709.
authors.forename: Geoffrey A
authors.initials: GA
authors.lastname: Mueller
authors.affiliation: Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina 27695.
authors.forename: Richele J
authors.initials: RJ
authors.lastname: Thompson
authors.affiliation: Medical Research Council Centre for Protein Engineering, Hills Road, Cambridge CB2 2QH, United Kingdom.
authors.forename: Alexey G
authors.initials: AG
authors.lastname: Murzin
authors.affiliation: Duke University NMR Center, Durham, North Carolina 27710.
authors.forename: Ronald A
authors.initials: RA
authors.lastname: Venters
authors.affiliation: Biomedical Sciences Department, Dental School, University of Maryland, Baltimore, Maryland 21201.
authors.forename: Mark A
authors.initials: MA
authors.lastname: Strauch
authors.affiliation: Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina 27695. Electronic address: john_cavanagh@ncsu.edu.
authors.forename: John
authors.initials: J
authors.lastname: Cavanagh
mesh_terms: D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology; D001426:Bacterial Proteins / Q000378:metabolism*; D003001:Cloning, Molecular; D004247:DNA / Q000737:chemistry*; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D003850:Deoxyribonuclease I / Q000737:chemistry; D066298:In Vitro Techniques; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D017386:Sequence Homology, Amino Acid; D014157:Transcription Factors / Q000378:metabolism*
chemical_list: C060762:AbrB protein, Bacillus subtilis; D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D014157:Transcription Factors; D004247:DNA; D003850:Deoxyribonuclease I