5MXN

Atomic model of the VipA/VipB/Hcp, the type six secretion system non-contractile sheath-tube of Vibrio cholerae from cryo-EM

Summary for 5MXN

• Entry DOI: 10.2210/pdb5mxn/pdb
• EMDB information: 3566
• Descriptor: Haemolysin co-regulated protein, Type VI secretion protein (3 entities in total)
• Functional Keywords: type iv secretion system, protein export, transport protein
• Biological source: Vibrio cholerae; More
• Total number of polymer chains: 18
• Total formula weight: 539426.39

Authors

Wang, J.,Brackmann, M.,Castano-Diez, D.,Kudryashev, M.,Goldie, K.,Maier, T.,Stahlberg, H.,Basler, M. (deposition date: 2017-01-23, release date: 2017-08-02, Last modification date: 2024-05-08)

Primary citation

Wang, J.,Brackmann, M.,Castano-Diez, D.,Kudryashev, M.,Goldie, K.N.,Maier, T.,Stahlberg, H.,Basler, M.
Cryo-EM structure of the extended type VI secretion system sheath-tube complex.
Nat Microbiol, 2:1507-1512, 2017

PubMed Abstract: The bacterial type VI secretion system (T6SS) uses contraction of a long sheath to quickly thrust a tube with associated effectors across membranes of eukaryotic and bacterial cells . Only limited structural information is available about the inherently unstable precontraction state of the T6SS. Here, we obtain a 3.7 Å resolution structure of a non-contractile sheath-tube complex using cryo-electron microscopy and show that it resembles the extended T6SS inside Vibrio cholerae cells. We build a pseudo-atomic model of the complete sheath-tube assembly, which provides a mechanistic understanding of coupling sheath contraction with pushing and rotating the inner tube for efficient target membrane penetration. Our data further show that sheath contraction exposes a buried recognition domain to specifically trigger the disassembly and recycling of the T6SS sheath by the cognate ATP-dependent unfoldase ClpV.

PubMed: 28947741
DOI: 10.1038/s41564-017-0020-7

Experimental method

ELECTRON MICROSCOPY (3.7 Å)