5U5O
Bacterial adhesin from Mobiluncus mulieris containing intramolecular disulfide, isopeptide, and ester bond cross-links (space group P1)
Summary for 5U5O
| Entry DOI | 10.2210/pdb5u5o/pdb |
| Related | 5U6F |
| Descriptor | LPXTG-motif cell wall anchor domain protein (2 entities in total) |
| Functional Keywords | bacterial adhesin, ig-like domain, intramolecular cross-link, cell adhesion |
| Biological source | Mobiluncus mulieris |
| Total number of polymer chains | 1 |
| Total formula weight | 31388.87 |
| Authors | Paynter, J.,Young, P.G.,Squire, C.J. (deposition date: 2016-12-07, release date: 2018-06-13, Last modification date: 2024-10-23) |
| Primary citation | Young, P.G.,Paynter, J.M.,Wardega, J.K.,Middleditch, M.J.,Payne, L.S.,Baker, E.N.,Squire, C.J. Domain structure and cross-linking in a giant adhesin from the Mobiluncus mulieris bacterium. Acta Crystallogr D Struct Biol, 79:971-979, 2023 Cited by PubMed Abstract: 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. PubMed: 37860959DOI: 10.1107/S2059798323007507 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.15 Å) |
Structure validation
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