5U6F

Bacterial adhesin from Mobiluncus mulieris containing intramolecular disulfide, isopeptide, and ester bond cross-links (space group P21)

5U6F の概要

• エントリーDOI: 10.2210/pdb5u6f/pdb
• 関連するPDBエントリー: 5U5O
• 分子名称: LPXTG-motif cell wall anchor domain protein (2 entities in total)
• 機能のキーワード: bacterial adhesin, ig-like domain, intramolecular cross-link, cell adhesion
• 由来する生物種: Mobiluncus mulieris
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31388.87

構造登録者

Paynter, J.,Young, P.G.,Squire, C.J. (登録日: 2016-12-07, 公開日: 2018-06-13, 最終更新日: 2024-10-09)

主引用文献

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

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: 37860959
DOI: 10.1107/S2059798323007507

実験手法

X-RAY DIFFRACTION (1.5 Å)