4CBV

X-ray structure of full-length ComE from Streptococcus pneumoniae.

4CBV の概要

• エントリーDOI: 10.2210/pdb4cbv/pdb
• 関連するPDBエントリー: 4ML3 4MLD
• 分子名称: COME (1 entity in total)
• 機能のキーワード: transcription, natural genetic transformation, transcription factor, rec domain
• 由来する生物種: STREPTOCOCCUS PNEUMONIAE
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 185866.71

構造登録者

Boudes, M.,Durand, D.,Graille, M.,van Tilbeurgh, H.,Quevillon-Cheruel, S. (登録日: 2013-10-16, 公開日: 2014-02-12, 最終更新日: 2024-11-06)

主引用文献

Boudes, M.,Sanchez, D.,Graille, M.,Van Tilbeurgh, H.,Durand, D.,Quevillon-Cheruel, S.
Structural Insights Into the Dimerization of the Response Regulator Come from Streptococcus Pneumoniae.
Nucleic Acids Res., 42:5302-, 2014

PubMed Abstract: Natural transformation contributes to the maintenance and to the evolution of the bacterial genomes. In Streptococcus pneumoniae, this function is reached by achieving the competence state, which is under the control of the ComD-ComE two-component system. We present the crystal and solution structures of ComE. We mimicked the active and non-active states by using the phosphorylated mimetic ComE(D58E) and the unphosphorylatable ComE(D58A) mutants. In the crystal, full-length ComE(D58A) dimerizes through its canonical REC receiver domain but with an atypical mode, which is also adopted by the isolated REC(D58A) and REC(D58E). The LytTR domain adopts a tandem arrangement consistent with the two direct repeats of its promoters. However ComE(D58A) is monomeric in solution, as seen by SAXS, by contrast to ComE(D58E) that dimerizes. For both, a relative mobility between the two domains is assumed. Based on these results we propose two possible ways for activation of ComE by phosphorylation.

PubMed: 24500202
DOI: 10.1093/NAR/GKU110

実験手法

X-RAY DIFFRACTION (3.39 Å)