8CW4

CryoEM structure of the N-pilus from Escherichia coli

これはPDB形式変換不可エントリーです。

8CW4 の概要

• エントリーDOI: 10.2210/pdb8cw4/pdb
• 関連するPDBエントリー: 8CUE
• EMDBエントリー: 26999 27023
• 分子名称: 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)
• 機能のキーワード: conjugation, tram, self transmissable plasmid, pili, structural protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 70
• 化学式量合計: 760904.90

構造登録者

Bui, K.H.,Black, C.S. (登録日: 2022-05-18, 公開日: 2023-02-01, 最終更新日: 2024-06-12)

主引用文献

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

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: 36513067
DOI: 10.1016/j.str.2022.11.007

実験手法

ELECTRON MICROSCOPY (3 Å)