1L0O

Crystal Structure of the Bacillus stearothermophilus Anti-Sigma Factor SpoIIAB with the Sporulation Sigma Factor SigmaF

1L0O の概要

• エントリーDOI: 10.2210/pdb1l0o/pdb
• 分子名称: Anti-sigma F factor, sigma factor, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: bergerat fold, helix-turn-helix, protein binding
• 由来する生物種: Geobacillus stearothermophilus; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 62374.72

構造登録者

Campbell, E.A.,Masuda, S.,Sun, J.L.,Muzzin, O.,Olson, C.A.,Wang, S.,Darst, S.A. (登録日: 2002-02-12, 公開日: 2002-04-03, 最終更新日: 2024-02-14)

主引用文献

Campbell, E.A.,Masuda, S.,Sun, J.L.,Muzzin, O.,Olson, C.A.,Wang, S.,Darst, S.A.
Crystal structure of the Bacillus stearothermophilus anti-sigma factor SpoIIAB with the sporulation sigma factor sigmaF.
Cell(Cambridge,Mass.), 108:795-807, 2002

PubMed Abstract: Cell type-specific transcription during Bacillus sporulation is established by sigmaF. SpoIIAB is an anti-sigma that binds and negatively regulates sigmaF, as well as a serine kinase that phosphorylates and inactivates the anti-anti-sigma SpoIIAA. The crystal structure of sigmaF bound to the SpoIIAB dimer in the low-affinity, ADP form has been determined at 2.9 A resolution. SpoIIAB adopts the GHKL superfamily fold of ATPases and histidine kinases. A domain of sigmaF contacts both SpoIIAB monomers, while 80% of the sigma factor is disordered. The interaction occludes an RNA polymerase binding surface of sigmaF, explaining the SpoIIAB anti-sigma activity. The structure also explains the specificity of SpoIIAB for its target sigma factors and, in combination with genetic and biochemical data, provides insight into the mechanism of SpoIIAA anti-anti-sigma activity.

PubMed: 11955433
DOI: 10.1016/S0092-8674(02)00662-1

実験手法

X-RAY DIFFRACTION (2.9 Å)