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Structure paper

TitleDual function of OmpM as outer membrane tether and nutrient uptake channel in diderm Firmicutes.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 7152, Year 2023
Publish dateNov 6, 2023
AuthorsAugustinas Silale / Yiling Zhu / Jerzy Witwinowski / Robert E Smith / Kahlan E Newman / Satya P Bhamidimarri / Arnaud Baslé / Syma Khalid / Christophe Beloin / Simonetta Gribaldo / Bert van den Berg /
PubMed AbstractThe outer membrane (OM) in diderm, or Gram-negative, bacteria must be tethered to peptidoglycan for mechanical stability and to maintain cell morphology. Most diderm phyla from the Terrabacteria ...The outer membrane (OM) in diderm, or Gram-negative, bacteria must be tethered to peptidoglycan for mechanical stability and to maintain cell morphology. Most diderm phyla from the Terrabacteria group have recently been shown to lack well-characterised OM attachment systems, but instead have OmpM, which could represent an ancestral tethering system in bacteria. Here, we have determined the structure of the most abundant OmpM protein from Veillonella parvula (diderm Firmicutes) by single particle cryogenic electron microscopy. We also characterised the channel properties of the transmembrane β-barrel of OmpM and investigated the structure and PG-binding properties of its periplasmic stalk region. Our results show that OM tethering and nutrient acquisition are genetically linked in V. parvula, and probably other diderm Terrabacteria. This dual function of OmpM may have played a role in the loss of the OM in ancestral bacteria and the emergence of monoderm bacterial lineages.
External linksNat Commun / PubMed:37932269 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.7 - 3.28 Å
Structure data

16328

8bym

EMDB-16328, PDB-8bym:
Outer membrane attachment porin OmpM1 from Veillonella parvula
Method: EM (single particle) / Resolution: 3.15 Å

16332

8bys

EMDB-16332, PDB-8bys:
Outer membrane attachment porin OmpM1 from Veillonella parvula, native
Method: EM (single particle) / Resolution: 3.28 Å

16333

8byt

EMDB-16333, PDB-8byt:
Outer membrane attachment porin OmpM1 from Veillonella parvula, C3 symmetry
Method: EM (single particle) / Resolution: 2.78 Å

PDB-8bz2:
Crystal structure of outer membrane attachment porin OmpM1 SLH domain
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • veillonella parvula (bacteria)
KeywordsMEMBRANE PROTEIN / Porin / outer membrane / attachment / peptidoglycan-binding / Outer membrane attachment / nutrient transport / STRUCTURAL PROTEIN

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