2MKY

Structure of the PrgK first periplasmic domain

Summary for 2MKY

• Entry DOI: 10.2210/pdb2mky/pdb
• NMR Information: BMRB: 19800
• Descriptor: Pathogenicity 1 island effector protein (1 entity in total)
• Functional Keywords: secretion systems, macromolecular assemblies, cell invasion
• Biological source: Salmonella enterica
• Total number of polymer chains: 1
• Total formula weight: 6532.36

Authors

Bergeron, J.,Mcintosh, L.,Strynadka, N. (deposition date: 2014-02-14, release date: 2014-10-29, Last modification date: 2024-05-01)

Primary citation

Bergeron, J.R.,Worrall, L.J.,De, S.,Sgourakis, N.G.,Cheung, A.H.,Lameignere, E.,Okon, M.,Wasney, G.A.,Baker, D.,McIntosh, L.P.,Strynadka, N.C.
The Modular Structure of the Inner-Membrane Ring Component PrgK Facilitates Assembly of the Type III Secretion System Basal Body.
Structure, 23:161-172, 2015

PubMed Abstract: The type III secretion system (T3SS) is a large macromolecular assembly found at the surface of many pathogenic Gram-negative bacteria. Its role is to inject toxic "effector" proteins into the cells of infected organisms. The molecular details of the assembly of this large, multimembrane-spanning complex remain poorly understood. Here, we report structural, biochemical, and functional analyses of PrgK, an inner-membrane component of the prototypical Salmonella typhimurium T3SS. We have obtained the atomic structures of the two ring building globular domains and show that the C-terminal transmembrane helix is not essential for assembly and secretion. We also demonstrate that structural rearrangement of the two PrgK globular domains, driven by an interconnecting linker region, may promote oligomerization into ring structures. Finally, we used electron microscopy-guided symmetry modeling to propose a structural model for the intimately associated PrgH-PrgK ring interaction within the assembled basal body.

PubMed: 25533490
DOI: 10.1016/j.str.2014.10.021

Experimental method

SOLUTION NMR