2KRF

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

2KRF の概要

• エントリーDOI: 10.2210/pdb2krf/pdb
• NMR情報: BMRB: 16636
• 分子名称: Transcriptional regulatory protein comA (1 entity in total)
• 機能のキーワード: activator, competence, dna-binding, transcription regulation, two-component regulatory system, transcription
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 16170.28

構造登録者

Hobbs, C.A.,Bobay, B.G.,Thompson, R.J.,Perego, M.,Cavanagh, J. (登録日: 2009-12-16, 公開日: 2010-04-07, 最終更新日: 2024-05-08)

主引用文献

Hobbs, C.A.,Bobay, B.G.,Thompson, R.J.,Perego, M.,Cavanagh, J.
NMR solution structure and DNA-binding model of the DNA-binding domain of competence protein A.
J.Mol.Biol., 398:248-263, 2010

PubMed Abstract: 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.

PubMed: 20302877
DOI: 10.1016/j.jmb.2010.03.003

実験手法

SOLUTION NMR