1SXI

Structure of apo transcription regulator B. megaterium

1SXI の概要

• エントリーDOI: 10.2210/pdb1sxi/pdb
• 関連するPDBエントリー: 1SXG 1SXH
• 分子名称: Glucose-resistance amylase regulator, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: allosterism; phosphoprotein; transcription regulation; gram positive bacteria; ccr, transcription
• 由来する生物種: Bacillus megaterium
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 376455.86

構造登録者

Schumacher, M.A.,Allen, G.S.,Diel, M.,Seidel, G.,Hillen, W.,Brennan, R.G. (登録日: 2004-03-30, 公開日: 2004-10-19, 最終更新日: 2024-11-13)

主引用文献

Schumacher, M.A.,Allen, G.S.,Diel, M.,Seidel, G.,Hillen, W.,Brennan, R.G.
Structural studies on the apo transcription factor form B. megaterium
Cell(Cambridge,Mass.), 118:731-741, 2004

PubMed Abstract: Carbon catabolite repression (CCR) is one of the most fundamental environmental-sensing mechanisms in bacteria and imparts competitive advantage by establishing priorities in carbon metabolism. In gram-positive bacteria, the master transcription regulator of CCR is CcpA. CcpA is a LacI-GalR family member that employs, as an allosteric corepressor, the phosphoprotein HPr-Ser46-P, which is formed in glucose-replete conditions. Here we report structures of the Bacillus megaterium apoCcpA and a CcpA-(HPr-Ser46-P)-DNA complex. These structures reveal that HPr-Ser46-P mediates a novel two-component allosteric DNA binding activation mechanism that involves both rotation of the CcpA subdomains and relocation of pivot-point residue Thr61, which leads to juxtaposition of the DNA binding regions permitting "hinge" helix formation in the presence of cognate DNA. The structure of the CcpA-(HPr-Ser46-P)-cre complex also reveals the elegant mechanism by which CcpA family-specific interactions with HPr-Ser46-P residues Ser46-P and His15 partition the high-energy CCR and low-energy PTS pathways, the latter requiring HPr-His15-P.

PubMed: 15369672
DOI: 10.1016/j.cell.2004.08.027

実験手法

X-RAY DIFFRACTION (3 Å)