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PDBsum entry 4d65

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Transport protein PDB id
4d65
Contents
Protein chains
(+ 0 more) 343 a.a.
Ligands
LDA ×165
FTT-MYR ×6
SO4 ×2
Waters ×3115

References listed in PDB file
Key reference
Title Porin self-Association enables cell-To-Cell contact inprovidencia stuartiifloating communities.
Authors M.El-Khatib, C.Nasrallah, J.Lopes, Q.T.Tran, G.Tetreau, H.Basbous, D.Fenel, B.Gallet, M.Lethier, J.M.Bolla, J.M.Pagès, M.Vivaudou, M.Weik, M.Winterhalter, J.P.Colletier.
Ref. Proc Natl Acad Sci U S A, 2018, 115, E2220. [DOI no: 10.1073/pnas.1714582115]
PubMed id 29476011
Abstract
The gram-negative pathogenProvidencia stuartiiforms 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 ofP. 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.
Secondary reference #1
Title Understanding voltage gating of providencia stuartii porins at atomic level.
Authors W.Song, H.Bajaj, C.Nasrallah, H.Jiang, M.Winterhalter, J.P.Colletier, Y.Xu.
Ref. PLoS Comput Biol, 2015, 11, e1004255.
PubMed id 25955156
Abstract
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