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8S7L

Crystal structure of a double mutant of VirB8-like OrfG central and C-terminal domains of Streptococcus thermophilus ICESt3 (Gram positive conjugative type IV secretion system).

Summary for 8S7L
Entry DOI10.2210/pdb8s7l/pdb
DescriptorPutative transfer protein (1 entity in total)
Functional Keywordstransport protein, virb8, gram-positive, t4ss
Biological sourceStreptococcus thermophilus
Total number of polymer chains3
Total formula weight92845.01
Authors
Favier, F.,Didierjean, C.,Maffo-Woulefack, R.,Douzi, B.,Leblond-Bourget, N. (deposition date: 2024-03-03, release date: 2025-03-12)
Primary citationMaffo-Woulefack, R.,Ali, A.M.,Laroussi, H.,Cappele, J.,Romero-Saavedra, F.,Ramia, N.,Robert, E.,Mathiot, S.,Soler, N.,Roussel, Y.,Fronzes, R.,Huebner, J.,Didierjean, C.,Favier, F.,Leblond-Bourget, N.,Douzi, B.
Elucidating assembly and function of VirB8 cell wall subunits refines the DNA translocation model in Gram-positive T4SSs.
Sci Adv, 11:eadq5975-eadq5975, 2025
Cited by
PubMed Abstract: Bacterial type IV secretion systems (T4SSs) are widespread nanomachines specialized in the transport across the cell envelope of various types of molecules including mobile genetic elements during conjugation. Despite their prevalence in Gram-positive bacteria, including relevant pathogens, their assembly and functioning remain unknown. This study addresses these gaps by investigating VirB8 proteins, known to be central components of conjugative T4SSs in Gram-positive bacteria. However, the functional packing and precise role of VirB8 in T4SSs biology remain undefined. Our findings elucidate the nature of VirB8 proteins as cell wall components, where they multimerize and exhibit a conserved assembly pattern, distinct from VirB8 in Gram-negative bacteria. We also demonstrate that VirB8 proteins interact with other T4SS subunits and DNA, indicating their pivotal role in the building of the DNA translocation channel across the cell wall. We lastly propose a distinct architecture for conjugative T4SSs in Gram-positive bacteria compared to their Gram-negative counterparts, possibly attributed to the differences in the cell wall structure.
PubMed: 39841841
DOI: 10.1126/sciadv.adq5975
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

237735

건을2025-06-18부터공개중

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