4d65

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

spinqualitylabelsall models 4d65, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4d65 is a 6 chain structure with sequence from Providencia stuartii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: FTT, LDA, MYR, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function E3U905_PROST Publication Abstract from PubMed The gram-negative pathogen Providencia stuartii 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 P. stuartii, 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. Porin self-association enables cell-to-cell contact in Providencia stuartii floating communities.,El-Khatib M, Nasrallah C, Lopes J, Tran QT, Tetreau G, Basbous H, Fenel D, Gallet B, Lethier M, Bolla JM, Pages JM, Vivaudou M, Weik M, Winterhalter M, Colletier JP Proc Natl Acad Sci U S A. 2018 Mar 6;115(10):E2220-E2228. doi:, 10.1073/pnas.1714582115. Epub 2018 Feb 23. PMID:29476011 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Porin 3D structures

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