5N9I

STRUCTURE OF 206-GVVTSE-211, THE STERIC ZIPPER THAT SUPPORTS THE SELF-ASSOCIATION OF P. STUARTII OMP-PST1 INTO DIMERS OF TRIMERS

Summary for 5N9I

• Entry DOI: 10.2210/pdb5n9i/pdb
• Descriptor: Porin 1 (2 entities in total)
• Functional Keywords: steric-zipper, porin, micro-crystal, self-association, cell adhesion
• Biological source: Providencia stuartii
• Cellular location: Cell outer membrane ; Multi-pass membrane protein : E3U904
• Total number of polymer chains: 4
• Total formula weight: 2362.50

Authors

Colletier, J.P.,Nasrallah, C. (deposition date: 2017-02-24, release date: 2018-02-21, Last modification date: 2024-05-01)

Primary citation

El-Khatib, M.,Nasrallah, C.,Lopes, J.,Tran, Q.T.,Tetreau, G.,Basbous, H.,Fenel, D.,Gallet, B.,Lethier, M.,Bolla, J.M.,Pages, J.M.,Vivaudou, M.,Weik, M.,Winterhalter, M.,Colletier, J.P.
Porin self-association enables cell-to-cell contact in
Proc. Natl. Acad. Sci. U.S.A., 115:E2220-E2228, 2018

PubMed Abstract: The gram-negative pathogen forms floating communities within which adjacent cells are in apparent contact, before depositing as canonical surface-attached biofilms. Because porins are the most abundant proteins in the outer membrane of gram-negative bacteria, we hypothesized that they could be involved in cell-to-cell contact and undertook a structure-function relationship study on the two porins of , Omp-Pst1 and Omp-Pst2. Our crystal structures reveal that these porins can self-associate through their extracellular loops, forming dimers of trimers (DOTs) that could enable cell-to-cell contact within floating communities. Support for this hypothesis was obtained by studying the porin-dependent aggregation of liposomes and model cells. The observation that facing channels are open in the two porin structures suggests that DOTs could not only promote cell-to-cell contact but also contribute to intercellular communication.

PubMed: 29476011
DOI: 10.1073/pnas.1714582115

Experimental method

X-RAY DIFFRACTION (1.91 Å)