PDBsum entry 5nxr

Cell adhesion

PDB id: 5nxr

Contents

Protein chains

352 a.a.

Ligands

LDA ×72

Metals

_CL

_CA

Waters ×834

PDB id:

5nxr

Name:

Cell adhesion

Title:

Trimeric structure of omp-pst1, the major porin from providencia stuartii

Structure:

Porin 1. Chain: a, c, b. Engineered: yes

Source:

Providencia stuartii. Organism_taxid: 588. Atcc: 29914. Expressed in: escherichia coli 'bl21-gold(de3)plyss ag'. Expression_system_taxid: 866768.

Resolution:

2.70Å R-factor: 0.240 R-free: 0.285

Authors:

J.P.Colletier,C.Nasrallah

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:

10-May-17 Release date: 21-Feb-18

Protein chains

E3U904  (E3U904_PROST) -  Porin 1 from Providencia stuartii

Seq: 374 a.a.

Struc: 352 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.