8QJA

T6SS-linked Rhs repeat protein - Advenella mimigardefordensis VgrG-Rhs core

Summary for 8QJA

• Entry DOI: 10.2210/pdb8qja/pdb
• Descriptor: Putative type VI secretion system YD repeat-containing Rhs element Vgr protein (1 entity in total)
• Functional Keywords: rhs, t6ss, vgrg-rhs, toxin cannister, rhs-repeat, cell invasion
• Biological source: Advenella mimigardefordensis DPN7
• Total number of polymer chains: 4
• Total formula weight: 851292.06

Authors

Kielkopf, C.S.,Shneider, M.M.,Leiman, P.G.,Taylor, N.M.I. (deposition date: 2023-09-13, release date: 2024-09-25, Last modification date: 2024-11-13)

Primary citation

Kielkopf, C.S.,Shneider, M.M.,Leiman, P.G.,Taylor, N.M.I.
T6SS-associated Rhs toxin-encapsulating shells: Structural and bioinformatical insights into bacterial weaponry and self-protection.
Structure, 2024

PubMed Abstract: Bacteria use the type VI secretion system (T6SS) to secrete toxins into pro- and eukaryotic cells via machinery consisting of a contractile sheath and a rigid tube. Rearrangement hotspot (Rhs) proteins represent one of the most common T6SS effectors. The Rhs C-terminal toxin domain displays great functional diversity, while the Rhs core is characterized by YD repeats. We elucidate the Rhs core structures of PAAR- and VgrG-linked Rhs proteins from Salmonella bongori and Advenella mimigardefordensis, respectively. The Rhs core forms a large shell of β-sheets with a negatively charged interior and encloses a large volume. The S. bongori Rhs toxin does not lead to ordered density in the Rhs shell, suggesting the toxin is unfolded. Together with bioinformatics analysis showing that Rhs toxins predominantly act intracellularly, this suggests that the Rhs core functions two-fold, as a safety feature for the producer cell and as delivery mechanism for the toxin.

PubMed: 39481373
DOI: 10.1016/j.str.2024.10.008

Experimental method

X-RAY DIFFRACTION (3.36 Å)