6TEA

Tail of native GTA particle computed with helical refinement, C6 symmetry

Summary for 6TEA

• Entry DOI: 10.2210/pdb6tea/pdb
• Related: 6TBA
• EMDB information: 10443 10478 10566
• Descriptor: Phage major tail protein, TP901-1 family (1 entity in total)
• Functional Keywords: "helical refinement", "tape measure protein", "bacteriophage", "tail tube", virus
• Biological source: Rhodobacter capsulatus
• Total number of polymer chains: 4
• Total formula weight: 57680.03

Authors

Bardy, P.,Fuzik, T.,Hrebik, D.,Pantucek, R.,Beatty, J.T.,Plevka, P. (deposition date: 2019-11-11, release date: 2020-07-22, Last modification date: 2024-05-22)

Primary citation

Bardy, P.,Fuzik, T.,Hrebik, D.,Pantucek, R.,Thomas Beatty, J.,Plevka, P.
Structure and mechanism of DNA delivery of a gene transfer agent.
Nat Commun, 11:3034-3034, 2020

PubMed Abstract: Alphaproteobacteria, which are the most abundant microorganisms of temperate oceans, produce phage-like particles called gene transfer agents (GTAs) that mediate lateral gene exchange. However, the mechanism by which GTAs deliver DNA into cells is unknown. Here we present the structure of the GTA of Rhodobacter capsulatus (RcGTA) and describe the conformational changes required for its DNA ejection. The structure of RcGTA resembles that of a tailed phage, but it has an oblate head shortened in the direction of the tail axis, which limits its packaging capacity to less than 4,500 base pairs of linear double-stranded DNA. The tail channel of RcGTA contains a trimer of proteins that possess features of both tape measure proteins of long-tailed phages from the family Siphoviridae and tail needle proteins of short-tailed phages from the family Podoviridae. The opening of a constriction within the RcGTA baseplate enables the ejection of DNA into bacterial periplasm.

PubMed: 32541663
DOI: 10.1038/s41467-020-16669-9

Experimental method

ELECTRON MICROSCOPY (3.89 Å)