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6TB9

Capsid of native GTA particle computed with C5 symmetry

This is a non-PDB format compatible entry.
Summary for 6TB9
Entry DOI10.2210/pdb6tb9/pdb
EMDB information10442 10443 10565 10592
DescriptorMajor capsid protein Rcc01687, Head spike base Rcc01079, Head spike fiber Rcc01080 (3 entities in total)
Functional Keywords"capsid", "gene transfer agent", "bacteriophage", "hk97", virus
Biological sourceRhodobacter capsulatus
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Total number of polymer chains42
Total formula weight1354621.40
Authors
Bardy, P.,Fuzik, T.,Hrebik, D.,Pantucek, R.,Beatty, J.T.,Plevka, P. (deposition date: 2019-11-01, release date: 2020-07-22, Last modification date: 2024-07-10)
Primary citationBardy, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.56 Å)
Structure validation

242500

数据于2025-10-01公开中

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