5MWW

Sigma1.1 domain of sigmaA from Bacillus subtilis

5MWW の概要

• エントリーDOI: 10.2210/pdb5mww/pdb
• NMR情報: BMRB: 34089
• 分子名称: RNA polymerase sigma factor SigA (1 entity in total)
• 機能のキーワード: autoinhibitor, transferase
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cytoplasm : A0A063XB56
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8977.56

構造登録者

Zachrdla, M.,Padrta, P.,Rabatinova, A.,Sanderova, H.,Barvik, I.,Krasny, L.,Zidek, L. (登録日: 2017-01-20, 公開日: 2017-06-14, 最終更新日: 2024-06-19)

主引用文献

Zachrdla, M.,Padrta, P.,Rabatinova, A.,Sanderova, H.,Barvik, I.,Krasny, L.,Zidek, L.
Solution structure of domain 1.1 of the sigma (A) factor from Bacillus subtilis is preformed for binding to the RNA polymerase core.
J. Biol. Chem., 292:11610-11617, 2017

PubMed Abstract: Bacterial RNA polymerase (RNAP) requires σ factors to recognize promoter sequences. Domain 1.1 of primary σ factors (σ1.1) prevents their binding to promoter DNA in the absence of RNAP, and when in complex with RNAP, it occupies the DNA-binding channel of RNAP. Currently, two 3D structures of σ1.1 are available: from in complex with RNAP and from solved free in solution. However, these two structures significantly differ, and it is unclear whether this difference is due to an altered conformation upon RNAP binding or to differences in intrinsic properties between the proteins from these two distantly related species. Here, we report the solution structure of σ1.1 from the Gram-positive bacterium We found that σ1.1 is highly compact because of additional stabilization not present in σ1.1 from the other two species and that it is more similar to σ1.1. Moreover, modeling studies suggested that σ1.1 requires minimal conformational changes for accommodating RNAP in the DNA channel, whereas σ1.1 must be rearranged to fit therein. Thus, the mesophilic species and share the same σ1.1 fold, whereas the fold of σ1.1 from the thermophile is distinctly different. Finally, we describe an intriguing similarity between σ1.1 and δ, an RNAP-associated protein in , bearing implications for the so-far unknown binding site of δ on RNAP. In conclusion, our results shed light on the conformational changes of σ1.1 required for its accommodation within bacterial RNAP.

PubMed: 28539362
DOI: 10.1074/jbc.M117.784074

実験手法

SOLUTION NMR