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-Structure paper
タイトル | Cryo-EM structure of the Agrobacterium tumefaciens T-pilus reveals the importance of positive charges in the lumen. |
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ジャーナル・号・ページ | Structure, Vol. 31, Issue 4, Page 375-384.e4, Year 2023 |
掲載日 | 2023年4月6日 |
著者 | Jaafar Amro / Corbin Black / Zakaria Jemouai / Nathan Rooney / Caroline Daneault / Natalie Zeytuni / Matthieu Ruiz / Khanh Huy Bui / Christian Baron / |
PubMed 要旨 | 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 ...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. |
リンク | Structure / PubMed:36513067 |
手法 | EM (単粒子) |
解像度 | 3.0 - 3.2 Å |
構造データ | EMDB-26999, PDB-8cue: EMDB-27023, PDB-8cw4: |
化合物 | ChemComp-CPL: ChemComp-PGW: |
由来 |
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キーワード | STRUCTURAL PROTEIN / conjugation / VirB2 / type IV secretion system / pili / TraM / self transmissable plasmid |