8DFK

X-ray crystal structure of Bacillus subtilis ComEA

8DFK の概要

• エントリーDOI: 10.2210/pdb8dfk/pdb
• 分子名称: ComE operon protein 1 (1 entity in total)
• 機能のキーワード: plasma membrane, dna binding, genetic competence, oligomerization, dna binding protein
• 由来する生物種: Bacillus subtilis subsp. subtilis
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 117162.84

構造登録者

Ahmed, I.,Khaja, F.T.,Neiditch, M.B. (登録日: 2022-06-22, 公開日: 2022-12-28, 最終更新日: 2024-05-22)

主引用文献

Ahmed, I.,Hahn, J.,Henrickson, A.,Khaja, F.T.,Demeler, B.,Dubnau, D.,Neiditch, M.B.
Structure-function studies reveal ComEA contains an oligomerization domain essential for transformation in gram-positive bacteria.
Nat Commun, 13:7724-7724, 2022

PubMed Abstract: An essential step in bacterial transformation is the uptake of DNA into the periplasm, across the thick peptidoglycan cell wall of Gram-positive bacteria, or the outer membrane and thin peptidoglycan layer of Gram-negative bacteria. ComEA, a DNA-binding protein widely conserved in transformable bacteria, is required for this uptake step. Here we determine X-ray crystal structures of ComEA from two Gram-positive species, Bacillus subtilis and Geobacillus stearothermophilus, identifying a domain that is absent in Gram-negative bacteria. X-ray crystallographic, genetic, and analytical ultracentrifugation (AUC) analyses reveal that this domain drives ComEA oligomerization, which we show is required for transformation. We use multi-wavelength AUC (MW-AUC) to characterize the interaction between DNA and the ComEA DNA-binding domain. Finally, we present a model for the interaction of the ComEA DNA-binding domain with DNA, suggesting that ComEA oligomerization may provide a pulling force that drives DNA uptake across the thick cell walls of Gram-positive bacteria.

PubMed: 36513643
DOI: 10.1038/s41467-022-35129-0

実験手法

X-RAY DIFFRACTION (3.2 Å)