8cw4

CryoEM structure of the N-pilus from Escherichia coli

spinqualitylabelsall models 8cw4, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8cw4 is a 70 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3Å Ligands: PGW Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q46696_ECOLX Publication Abstract from PubMed Agrobacterium 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 Agrobacterium tumefaciens 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. 2023 Apr 6;31(4):375-384.e4. doi: 10.1016/j.str.2022.11.007. Epub 2022 , Dec 12. PMID:36513067 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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