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TitleA shared mechanism for Bacteroidota protein transport and gliding motility.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 10217, Year 2025
Publish dateNov 20, 2025
AuthorsXiaolong Liu / Marieta Avramova / Justin C Deme / Rachel L Jones / Camilla A K Lundgren / Susan M Lea / Ben C Berks /
PubMed AbstractBacteria of the phylum Bacteroidota are major human commensals and pathogens in addition to being abundant members of the wider biosphere. Bacteroidota move by gliding and they export proteins using ...Bacteria of the phylum Bacteroidota are major human commensals and pathogens in addition to being abundant members of the wider biosphere. Bacteroidota move by gliding and they export proteins using the Type 9 Secretion System (T9SS). Here we discover that gliding motility and the T9SS share an unprecedented mechanism of energisation in which outer membrane proteins are covalently attached by disulfide bonds to a moving internal track structure that propels them laterally through the membrane. We determined the structure of an exemplar Bacteroidota mobile track by obtaining the cryoEM structure of a 3 MDa circular mini-track from Porphyromonas gingivalis. Our discoveries identify a mechanistic and evolutionary link between gliding motility and T9SS-dependent protein transport.
External linksNat Commun / PubMed:41266322 / PubMed Central
MethodsEM (single particle)
Resolution2.7 - 3.7 Å
Structure data

48835

9n2d

EMDB-48835, PDB-9n2d:
Cryo-EM structure of an extended F. johnsoniae BAM complex, composite map
Method: EM (single particle) / Resolution: 2.7 Å

48836

9n2e

EMDB-48836, PDB-9n2e:
Cryo-EM structure of F. johnsoniae BamAP
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

ChemComp-DGA:
DIACYL GLYCEROL

ChemComp-JSG:
(2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-2-[(2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-5-[(2~{S},3~{S},4~{R},5~{R},6~{R})-6-[(1~{S})-1,2-bis(oxidanyl)ethyl]-4-[(2~{R},3~{S},4~{R},5~{S},6~{R})-6-[(1~{S})-2-[(2~{S},3~{S},4~{S},5~{S},6~{R})-6-[(1~{S})-1,2-bis(oxidanyl)ethyl]-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-1-oxidanyl-ethyl]-3,4-bis(oxidanyl)-5-phosphonooxy-oxan-2-yl]oxy-3-oxidanyl-5-phosphonooxy-oxan-2-yl]oxy-2-carboxy-2-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-5-[[(3~{R})-3-dodecanoyloxytetradecanoyl]amino]-6-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-3-oxidanyl-5-[[(3~{R})-3-oxidanyltetradecanoyl]amino]-4-[(3~{R})-3-oxidanyltetradecanoyl]oxy-6-phosphonooxy-oxan-2-yl]methoxy]-3-phosphonooxy-4-[(3~{R})-3-tetradecanoyloxytetradecanoyl]oxy-oxan-2-yl]methoxy]oxan-4-yl]oxy-4,5-bis(oxidanyl)oxane-2-carboxylic acid

ChemComp-PTY:
PHOSPHATIDYLETHANOLAMINE / phospholipid*YM

ChemComp-MAN:
alpha-D-mannopyranose

ChemComp-PLM:
PALMITIC ACID

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • flavobacterium johnsoniae uw101 (bacteria)
KeywordsMEMBRANE PROTEIN / BAM complex / BamA / BamD / BamG / BamH / BamM / BamP / outer-membrane proteins / OMP / BamAP complex

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