5u5o | pdb_00005u5o

Bacterial adhesin from Mobiluncus mulieris containing intramolecular disulfide, isopeptide, and ester bond cross-links (space group P1)

spinqualitylabelsall models 5u5o, resolution 1.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5u5o is a 1 chain structure with sequence from Mobiluncus mulieris. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.15Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function E0QN07_9ACTO Publication Abstract from PubMed 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. Domain structure and cross-linking in a giant adhesin from the Mobiluncus mulieris bacterium.,Young PG, Paynter JM, Wardega JK, Middleditch MJ, Payne LS, Baker EN, Squire CJ Acta Crystallogr D Struct Biol. 2023 Nov 1;79(Pt 11):971-979. doi: , 10.1107/S2059798323007507. Epub 2023 Oct 20. PMID:37860959 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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