PDBsum entry 4d65

Transport protein

PDB id: 4d65

Contents

Protein chains

(+ 0 more) 343 a.a.

Ligands

LDA ×165

FTT-MYR ×6

SO4 ×2

Waters ×3115

PDB id:

4d65

Name:

Transport protein

Title:

Structure of porin omp-pst2 from p. Stuartii; the asymmetric unit contains a dimer of trimers.

Structure:

Porin 2. Chain: a, b, c, d, e, f. Engineered: yes

Source:

Providencia stuartii. Organism_taxid: 588. Atcc: 29914. Expressed in: escherichia coli. Expression_system_taxid: 511693. Expression_system_variant: delta-omp8.

Resolution:

2.20Å R-factor: 0.168 R-free: 0.197

Authors:

C.Nasrallah,J.P.Colletier

Key ref:

M.El-Khatib et al. (2018). Porin self-association enables cell-to-cell contact inProvidencia stuartiifloating communities. Proc Natl Acad Sci U S A, 115, E2220. PubMed id: 29476011 DOI: 10.1073/pnas.1714582115

Date:

08-Nov-14 Release date: 09-Mar-16

Protein chains

E3U905  (E3U905_PROST) -  Porin 2 from Providencia stuartii

Seq: 365 a.a.

Struc: 343 a.a.

DOI no: 10.1073/pnas.1714582115

Proc Natl Acad Sci U S A 115:E2220 (2018)

PubMed id: 29476011

Porin self-association enables cell-to-cell contact inProvidencia stuartiifloating communities.

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.

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.