1FSP

NMR SOLUTION STRUCTURE OF BACILLUS SUBTILIS SPO0F PROTEIN, 20 STRUCTURES

1FSP の概要

• エントリーDOI: 10.2210/pdb1fsp/pdb
• 分子名称: STAGE 0 SPORULATION PROTEIN F (1 entity in total)
• 機能のキーワード: response regulator, sporulation, two-component systems, bacterial signal transduction, phospho-relay, (beta/alpha)5 protein
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cytoplasm (Probable): P06628
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14244.66

構造登録者

Feher, V.A.,Skelton, N.J.,Dahlquist, F.W.,Cavanagh, J. (登録日: 1997-06-05, 公開日: 1997-12-10, 最終更新日: 2024-05-22)

主引用文献

Feher, V.A.,Zapf, J.W.,Hoch, J.A.,Whiteley, J.M.,McIntosh, L.P.,Rance, M.,Skelton, N.J.,Dahlquist, F.W.,Cavanagh, J.
High-resolution NMR structure and backbone dynamics of the Bacillus subtilis response regulator, Spo0F: implications for phosphorylation and molecular recognition.
Biochemistry, 36:10015-10025, 1997

PubMed Abstract: NMR has been employed for structural and dynamic studies of the bacterial response regulator, Spo0F. This 124-residue protein is an essential component of the sporulation phosphorelay signal transduction pathway in Bacillus subtilis. Three-dimensional 1H, 15N, and 13C experiments have been used to obtain full side chain assignments and the 1511 distance, 121 dihedral angle, and 80 hydrogen bonding restraints required for generating a family of structures (14 restraints per residue). The structures give a well-defined (alpha/beta)5 fold for residues 4-120 with average rms deviations of 0.59 A for backbone heavy atoms and 1.02 A for all heavy atoms. Analyses of backbone 15N relaxation measurements demonstrate relative rigidity in most regions of regular secondary structure with a generalized order parameter (S2) of 0.9 +/- 0.05 and a rotational correlation time (taum) of 7.0 +/- 0.5 ns. Loop regions near the site of phosphorylation have higher than average rms deviation values and T1/T2 ratios suggesting significant internal motion or chemical exchange at these sites. Additionally, multiple conformers are observed for the beta4-alpha4 loop and beta-strand 5 region. These conformers may be related to structural changes associated with phosphorylation and also indicative of the propensity this recognition surface has for differential protein interactions. Comparison of Spo0F structural features to those of other response regulators reveals subtle differences in the orientations of secondary structure in the putative recognition surfaces and the relative charge distribution of residues surrounding the site of phosphorylation. These may be important in providing specificity for protein-protein interactions and for determining the lifetimes of the phosphorylated state.

PubMed: 9254596
DOI: 10.1021/bi970816l

実験手法

SOLUTION NMR