1BUZ
SOLUTION STRUCTURE OF SPOIIAA, A PHOSPHORYLATABLE COMPONENT OF THE SYSTEM THAT REGULATES TRANSCRIPTION FACTOR SIGMA-F OF BACILLUS SUBTILIS NMR, MINIMIZED AVERAGE STRUCTURE
1BUZ の概要
| エントリーDOI | 10.2210/pdb1buz/pdb |
| 分子名称 | SPOIIAA (1 entity in total) |
| 機能のキーワード | transcription regulator, kinase substrate, anti-anti sigma factor, novel alpha/beta fold, sporulation, phosphorylation |
| 由来する生物種 | Bacillus subtilis |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 12874.98 |
| 構造登録者 | Kovacs, H.,Comfort, D.,Lord, M.,Campbell, I.D.,Yudkin, M.D. (登録日: 1997-09-08, 公開日: 1998-07-01, 最終更新日: 2024-04-10) |
| 主引用文献 | Kovacs, H.,Comfort, D.,Lord, M.,Campbell, I.D.,Yudkin, M.D. Solution structure of SpoIIAA, a phosphorylatable component of the system that regulates transcription factor sigmaF of Bacillus subtilis. Proc.Natl.Acad.Sci.USA, 95:5067-5071, 1998 Cited by PubMed Abstract: The establishment of differential gene expression in sporulating Bacillus subtilis involves four protein components, one of which, SpoIIAA, undergoes phosphorylation and dephosphorylation. We have used NMR spectroscopy to determine the solution structure of the nonphosphorylated form of SpoIIAA. The structure shows a fold consisting of a four-stranded beta-sheet and four alpha-helices. Knowledge of the structure helps to account for the phenotype of several strains of B. subtilis that carry known spoIIAA mutations and should facilitate investigations of the conformational consequences of phosphorylation. PubMed: 9560229DOI: 10.1073/pnas.95.9.5067 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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