4D65

Structure of porin Omp-Pst2 from P. stuartii; the asymmetric unit contains a dimer of trimers.

Summary for 4D65

• Entry DOI: 10.2210/pdb4d65/pdb
• Related: 4D5X 4D64
• Descriptor: PORIN 2, LAURYL DIMETHYLAMINE-N-OXIDE, 3-HYDROXY-TETRADECANOIC ACID, ... (6 entities in total)
• Functional Keywords: transport protein, steric-zipper, bacterial junction, dimer of trimers
• Biological source: PROVIDENCIA STUARTII
• Total number of polymer chains: 6
• Total formula weight: 268527.01

Authors

Nasrallah, C.,Colletier, J.P. (deposition date: 2014-11-08, release date: 2016-03-09, Last modification date: 2023-12-20)

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 inProvidencia stuartiifloating communities.
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 (2.2 Å)