6NM5 の概要
エントリーDOI | 10.2210/pdb6nm5/pdb |
関連するPDBエントリー | 6NM5 |
EMDBエントリー | 0448 0450 0451 9397 9399 |
分子名称 | Type IV conjugative transfer system pilin TraA, Maturation protein, (2R)-2,3-dihydroxypropyl ethyl hydrogen (S)-phosphate (3 entities in total) |
機能のキーワード | ms2 maturation protein, f-pilus, adsorption complex, protein binding |
由来する生物種 | Escherichia coli 詳細 |
タンパク質・核酸の鎖数 | 76 |
化学式量合計 | 570381.02 |
構造登録者 | |
主引用文献 | Meng, R.,Jiang, M.,Cui, Z.,Chang, J.Y.,Yang, K.,Jakana, J.,Yu, X.,Wang, Z.,Hu, B.,Zhang, J. Structural basis for the adsorption of a single-stranded RNA bacteriophage. Nat Commun, 10:3130-3130, 2019 Cited by PubMed Abstract: Single-stranded RNA bacteriophages (ssRNA phages) infect Gram-negative bacteria via a single maturation protein (Mat), which attaches to a retractile pilus of the host. Here we present structures of the ssRNA phage MS2 in complex with the Escherichia coli F-pilus, showing a network of hydrophobic and electrostatic interactions at the Mat-pilus interface. Moreover, binding of the pilus induces slight orientational variations of the Mat relative to the rest of the phage capsid, priming the Mat-connected genomic RNA (gRNA) for its release from the virions. The exposed tip of the attached Mat points opposite to the direction of the pilus retraction, which may facilitate the translocation of the gRNA from the capsid into the host cytosol. In addition, our structures determine the orientation of the assembled F-pilin subunits relative to the cell envelope, providing insights into the F-like type IV secretion systems. PubMed: 31311931DOI: 10.1038/s41467-019-11126-8 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (6.2 Å) |
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