2krf | pdb_00002krf

NMR solution structure of the DNA binding domain of Competence protein A

spinqualitylabelsall models 2krf Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2krf is a 2 chain structure with sequence from Bacillus subtilis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CMPA_BACSU Response regulator in the two-component regulatory system ComP/ComA involved in a major quorum response pathway that regulates the development of genetic competence. Regulates directly the expression of over 20 genes, including genes of the srfA operon, degQ, rapA, rapC, rapE, rapF, etc. Regulates indirectly, through the regulation of comK transcription, the expression of late competence genes. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Competence protein A (ComA) is a response regulator protein involved in the development of genetic competence in the Gram-positive spore-forming bacterium Bacillus subtilis, as well as the regulation of the production of degradative enzymes and antibiotic synthesis. ComA belongs to the NarL family of proteins, which are characterized by a C-terminal transcriptional activator domain that consists of a bundle of four helices, where the second and third helices (alpha 8 and alpha 9) form a helix-turn-helix DNA-binding domain. Using NMR spectroscopy, the high-resolution 3D solution structure of the C-terminal DNA-binding domain of ComA (ComAC) has been determined. In addition, surface plasmon resonance and NMR protein-DNA titration experiments allowed for the analysis of the interaction of ComAC with its target DNA sequences. Combining the solution structure and biochemical data, a model of ComAC bound to the ComA recognition sequences on the srfA promoter has been developed. The model shows that for DNA binding, ComA uses the conserved helix-turn-helix motif present in other NarL family members. However, the model reveals also that ComA might use a slightly different part of the helix-turn-helix motif and there appears to be some associated domain re-orientation. These observations suggest a basis for DNA binding specificity within the NarL family. NMR solution structure and DNA-binding model of the DNA-binding domain of competence protein A.,Hobbs CA, Bobay BG, Thompson RJ, Perego M, Cavanagh J J Mol Biol. 2010 Apr 30;398(2):248-63. Epub 2010 Mar 17. PMID:20302877 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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