7P0H

Crystal structure of Helicobacter pylori ComF fused to an artificial alphaREP crystallization helper(named B2)

Summary for 7P0H

• Entry DOI: 10.2210/pdb7p0h/pdb
• Descriptor: Helicobacter pylori ComF fused to an artificial alphaREP crystallization helper (named B2), ZINC ION, 1-O-pyrophosphono-5-O-phosphono-alpha-D-ribofuranose, ... (6 entities in total)
• Functional Keywords: competence protein, recombination
• Biological source: Synthetic construct; More
• Total number of polymer chains: 4
• Total formula weight: 191792.24

Authors

Celma, L.,Walbott, H.,Legrand, P.,Quevillon-Cheruel, S. (deposition date: 2021-06-29, release date: 2022-04-06, Last modification date: 2024-10-09)

Primary citation

Damke, P.P.,Celma, L.,Kondekar, S.M.,Di Guilmi, A.M.,Marsin, S.,Depagne, J.,Veaute, X.,Legrand, P.,Walbott, H.,Vercruyssen, J.,Guerois, R.,Quevillon-Cheruel, S.,Radicella, J.P.
ComFC mediates transport and handling of single-stranded DNA during natural transformation.
Nat Commun, 13:1961-1961, 2022

PubMed Abstract: The ComFC protein is essential for natural transformation, a process that plays a major role in the spread of antibiotic resistance genes and virulence factors across bacteria. However, its role remains largely unknown. Here, we show that Helicobacter pylori ComFC is involved in DNA transport through the cell membrane, and is required for the handling of the single-stranded DNA once it is delivered into the cytoplasm. The crystal structure of ComFC includes a zinc-finger motif and a putative phosphoribosyl transferase domain, both necessary for the protein's in vivo activity. Furthermore, we show that ComFC is a membrane-associated protein with affinity for single-stranded DNA. Our results suggest that ComFC provides the link between the transport of the transforming DNA into the cytoplasm and its handling by the recombination machinery.

PubMed: 35414142
DOI: 10.1038/s41467-022-29494-z

Experimental method

X-RAY DIFFRACTION (2.499 Å)