2YAL

SinR, Master Regulator of biofilm formation in Bacillus subtilis

2YAL の概要

• エントリーDOI: 10.2210/pdb2yal/pdb
• 関連するPDBエントリー: 1B0N
• 分子名称: HTH-TYPE TRANSCRIPTIONAL REGULATOR SINR, NICKEL (II) ION (2 entities in total)
• 機能のキーワード: transcription, transcription regulator, antagonist, sporulation
• 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: 9941.80

構造登録者

Colledge, V.L.,Fogg, M.J.,Levdikov, V.M.,Leech, A.,Dodson, E.J.,Wilkinson, A.J. (登録日: 2011-02-23, 公開日: 2011-06-08, 最終更新日: 2023-12-20)

主引用文献

Colledge, V.L.,Fogg, M.J.,Levdikov, V.M.,Leech, A.,Dodson, E.J.,Wilkinson, A.J.
Structure and Organisation of Sinr, the Master Regulator of Biofilm Formation in Bacillus Subtilis.
J.Mol.Biol., 411:597-, 2011

PubMed Abstract: sinR encodes a tetrameric repressor of genes required for biofilm formation in Bacillus subtilis. sinI, which is transcribed under Spo0A control, encodes a dimeric protein that binds to SinR to form a SinR-SinI heterodimer in which the DNA-binding functions of SinR are abrogated and repression of biofilm genes is relieved. The heterodimer-forming surface comprises residues conserved between SinR and SinI. Each forms a pair of α-helices that hook together to form an intermolecular four-helix bundle. Here, we are interested in the assembly of the SinR tetramer and its binding to DNA. Size-exclusion chromatography with multi-angle laser light scattering and crystallographic analysis reveal that a DNA-binding fragment of SinR (residues 1-69) is a monomer, while a SinI-binding fragment (residues 74-111) is a tetramer arranged as a dimer of dimers. The SinR(74-111) chain forms two α-helices with the organisation of the dimer similar to that observed in the SinR-SinI complex. The tetramer is formed through interactions of residues at the C-termini of the four chains. A model of the intact SinR tetramer in which the DNA binding domains surround the tetramerisation core was built. Fluorescence anisotropy and surface plasmon resonance experiments showed that SinR binds to an oligonucleotide duplex, 5'-TTTGTTCTCTAAAGAGAACTTA-3', containing a pair of SinR consensus sequences in inverted orientation with a K(d) of 300 nM. The implications of these data for promoter binding and the curious quaternary structural transitions of SinR upon binding to (i) SinI and (ii) the SinR-like protein SlrR, which "repurposes" SinR as a repressor of autolysin and motility genes, are discussed.

PubMed: 21708175
DOI: 10.1016/J.JMB.2011.06.004

実験手法

X-RAY DIFFRACTION (2.27 Å)