6NM5

F-pilus/MS2 Maturation protein complex

This is a non-PDB format compatible entry.

Summary for 6NM5

• Entry DOI: 10.2210/pdb6nm5/pdb
• Related: 6NM5
• EMDB information: 0448 0450 0451 9397 9399
• Descriptor: Type IV conjugative transfer system pilin TraA, Maturation protein, (2R)-2,3-dihydroxypropyl ethyl hydrogen (S)-phosphate (3 entities in total)
• Functional Keywords: ms2 maturation protein, f-pilus, adsorption complex, protein binding
• Biological source: Escherichia coli; More
• Total number of polymer chains: 76
• Total formula weight: 570381.02

Authors

Meng, R.,Chang, J.,Zhang, J. (deposition date: 2019-01-10, release date: 2019-07-24, Last modification date: 2024-03-20)

Primary citation

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

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: 31311931
DOI: 10.1038/s41467-019-11126-8

Experimental method

ELECTRON MICROSCOPY (6.2 Å)