8cue
From Proteopedia
CryoEM structure of the T-pilus from Agrobacterium tumefaciens
Structural highlights
FunctionVIRB2_AGRFC VirB proteins are suggested to act at the bacterial surface and there play an important role in directing T-DNA transfer to plant cells. Publication Abstract from PubMedAgrobacterium tumefaciens is a natural genetic engineer that transfers DNA into plants, which is the most applied process for generation of genetically modified plants. DNA transfer is mediated by a type IV secretion system in the cell envelope and extracellular T-pili. We here report the cryo-electron microscopic structures of the T-pilus at 3.2-A resolution and of the plasmid pKM101-determined N-pilus at 3-A resolution. Both pili contain a main pilus protein (VirB2 in A. tumefaciens, TraM in pKM101) and phospholipids arranged in a five-start helical assembly. They contain positively charged amino acids in the lumen, and the lipids are positively charged in the T-pilus (phosphatidylcholine) conferring overall positive charge. Mutagenesis of the lumen-exposed Arg91 in VirB2 results in protein destabilization and loss of pilus formation. Our results reveal that different phospholipids can be incorporated into type IV secretion pili and that the charge of the lumen may be of functional importance. Cryo-EM structure of the Agrobacteriumtumefaciens T-pilus reveals the importance of positive charges in the lumen.,Amro J, Black C, Jemouai Z, Rooney N, Daneault C, Zeytuni N, Ruiz M, Bui KH, Baron C Structure. 2022 Dec 5:S0969-2126(22)00456-7. doi: 10.1016/j.str.2022.11.007. PMID:36513067[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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