Domain structure and cross-linking in a giant adhesin from the Mobiluncus mulieris bacterium.
Ig-like domains
bacterial adhesins
cell adhesion
intramolecular cross-links
Journal
Acta crystallographica. Section D, Structural biology
ISSN: 2059-7983
Titre abrégé: Acta Crystallogr D Struct Biol
Pays: United States
ID NLM: 101676043
Informations de publication
Date de publication:
01 Nov 2023
01 Nov 2023
Historique:
received:
16
06
2023
accepted:
27
08
2023
medline:
2
11
2023
pubmed:
20
10
2023
entrez:
20
10
2023
Statut:
ppublish
Résumé
Cell-surface proteins known as adhesins enable bacteria to colonize particular environments, and in Gram-positive bacteria often contain autocatalytically formed covalent intramolecular cross-links. While investigating the prevalence of such cross-links, a remarkable example was discovered in Mobiluncus mulieris, a pathogen associated with bacterial vaginosis. This organism encodes a putative adhesin of 7651 residues. Crystallography and mass spectrometry of two selected domains, and AlphaFold structure prediction of the remainder of the protein, were used to show that this adhesin belongs to the family of thioester, isopeptide and ester-bond-containing proteins (TIE proteins). It has an N-terminal domain homologous to thioester adhesion domains, followed by 51 immunoglobulin (Ig)-like domains containing ester- or isopeptide-bond cross-links. The energetic cost to the M. mulieris bacterium in retaining such a large adhesin as a single gene or protein construct suggests a critical role in pathogenicity and/or persistence.
Identifiants
pubmed: 37860959
pii: S2059798323007507
doi: 10.1107/S2059798323007507
pmc: PMC10619420
doi:
Substances chimiques
Adhesins, Bacterial
0
Esters
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
971-979Subventions
Organisme : Marsden Fund
ID : UOA1421
Informations de copyright
open access.
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