6U9E

Structure of PdpA-VgrG Complex, Lidless

Summary for 6U9E

• Entry DOI: 10.2210/pdb6u9e/pdb
• EMDB information: 20695 20696 20698
• Descriptor: PdpA, VgrG (2 entities in total)
• Functional Keywords: t6ss central spike, complex, transport protein
• Biological source: Francisella novicida; More
• Total number of polymer chains: 6
• Total formula weight: 348029.22

Authors

Yang, X.,Clemens, D.L.,Lee, B.-Y.,Cui, Y.,Zhou, Z.H.,Horwitz, M.A. (deposition date: 2019-09-08, release date: 2019-10-23, Last modification date: 2024-03-20)

Primary citation

Yang, X.,Clemens, D.L.,Lee, B.Y.,Cui, Y.,Zhou, Z.H.,Horwitz, M.A.
Atomic Structure of the Francisella T6SS Central Spike Reveals a Unique alpha-Helical Lid and a Putative Cargo.
Structure, 27:1811-1819.e6, 2019

PubMed Abstract: Francisella bacteria rely on a phylogenetically distinct type VI secretion system (T6SS) to escape host phagosomes and cause the fatal disease tularemia, but the structural and molecular mechanisms involved are unknown. Here we report the atomic structure of the Francisella T6SS central spike complex, obtained by cryo-electron microscopy. Our structural and functional studies demonstrate that, unlike the single-protein spike composition of other T6SS subtypes, Francisella T6SS's central spike is formed by two proteins, PdpA and VgrG, akin to T4-bacteriophage gp27 and gp5, respectively, and that PdpA has unique characteristics, including a putative cargo within its cavity and an N-terminal helical lid. Structure-guided mutagenesis demonstrates that the PdpA N-terminal lid and C-terminal spike are essential to Francisella T6SS function. PdpA is thus both an adaptor, connecting VgrG to the tube, and a likely carrier of secreted cargo. These findings are important to understanding Francisella pathogenicity and designing therapeutics to combat tularemia.

PubMed: 31677891
DOI: 10.1016/j.str.2019.10.007

Experimental method

ELECTRON MICROSCOPY (4.21 Å)