7AED

VirB8 domain of PrgL from Enterococcus faecalis pCF10

Summary for 7AED

• Entry DOI: 10.2210/pdb7aed/pdb
• Descriptor: PrgL, 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL (3 entities in total)
• Functional Keywords: conjugation, t4ss, virb8, membrane protein
• Biological source: Enterococcus faecalis
• Total number of polymer chains: 2
• Total formula weight: 45500.59

Authors

Jaeger, F.,Berntsson, R.P.A. (deposition date: 2020-09-17, release date: 2020-11-18, Last modification date: 2024-06-19)

Primary citation

Jager, F.,Lamy, A.,Sun, W.S.,Guerini, N.,Berntsson, R.P.
Structure of the enterococcal T4SS protein PrgL reveals unique dimerization interface in the VirB8 protein family.
Structure, 30:876-, 2022

PubMed Abstract: Multidrug-resistant bacteria pose serious problems in hospital-acquired infections (HAIs). Most antibiotic resistance genes are acquired via conjugative gene transfer, mediated by type 4 secretion systems (T4SS). Although most multidrug-resistant bacteria responsible for HAIs are of Gram-positive origin, with enterococci being major contributors, mostly Gram-negative T4SSs have been characterized. Here, we describe the structure and organization of PrgL, a core protein of the T4SS channel, encoded by the pCF10 plasmid from Enterococcus faecalis. The structure of PrgL displays similarity to VirB8 proteins of Gram-negative T4SSs. In vitro experiments show that the soluble domain alone is enough to drive both dimerization and dodecamerization, with a dimerization interface that differs from all other known VirB8-like proteins. In vivo experiments verify the importance of PrgL dimerization. Our findings provide insight into the molecular building blocks of Gram-positive T4SS, highlighting similarities but also unique features in PrgL compared to other VirB8-like proteins.

PubMed: 35429437
DOI: 10.1016/j.str.2022.03.013

Experimental method

X-RAY DIFFRACTION (1.753 Å)