8DSS

X-ray crystal structure of Geobacillus stearothermophilus ComEA

Summary for 8DSS

• Entry DOI: 10.2210/pdb8dss/pdb
• Related: 8DFK
• Descriptor: ComE operon protein 1 (2 entities in total)
• Functional Keywords: plasma membrane, dna binding, genetic competence, oligomerization, dna binding protein
• Biological source: Geobacillus stearothermophilus ATCC 7953
• Total number of polymer chains: 2
• Total formula weight: 31313.45

Authors

Ahmed, I.,Neiditch, M.B. (deposition date: 2022-07-22, release date: 2022-12-28, Last modification date: 2023-10-25)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.05 Å)