Summary for 8CW4
| Entry DOI | 10.2210/pdb8cw4/pdb |
| Related | 8CUE |
| EMDB information | 26999 27023 |
| Descriptor | Conjugal transfer protein TraM, (1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(hexadecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate (2 entities in total) |
| Functional Keywords | conjugation, tram, self transmissable plasmid, pili, structural protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 70 |
| Total formula weight | 760904.90 |
| Authors | Bui, K.H.,Black, C.S. (deposition date: 2022-05-18, release date: 2023-02-01, Last modification date: 2024-06-12) |
| Primary citation | Amro, J.,Black, C.,Jemouai, Z.,Rooney, N.,Daneault, C.,Zeytuni, N.,Ruiz, M.,Bui, K.H.,Baron, C. Cryo-EM structure of the Agrobacterium tumefaciens T-pilus reveals the importance of positive charges in the lumen. Structure, 31:375-384.e4, 2023 Cited by PubMed Abstract: 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-Å resolution and of the plasmid pKM101-determined N-pilus at 3-Å 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. PubMed: 36513067DOI: 10.1016/j.str.2022.11.007 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
Download full validation report
