5OX7

Structure of P110 from Mycoplasma genitalium at 2.4A with potassium ion

5OX7 の概要

• エントリーDOI: 10.2210/pdb5ox7/pdb
• 関連するPDBエントリー: 5MZ9 5MZB 5MZD
• 分子名称: Mgp-operon protein 3, POTASSIUM ION (3 entities in total)
• 機能のキーワード: mycoplasma genitalium protein d, cell adhesion
• 由来する生物種: Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 99594.30

構造登録者

Aparicio, D.,Fita, I. (登録日: 2017-09-06, 公開日: 2018-10-10, 最終更新日: 2024-01-17)

主引用文献

Aparicio, D.,Torres-Puig, S.,Ratera, M.,Querol, E.,Pinol, J.,Pich, O.Q.,Fita, I.
Mycoplasma genitalium adhesin P110 binds sialic-acid human receptors.
Nat Commun, 9:4471-4471, 2018

PubMed Abstract: Adhesion of pathogenic bacteria to target cells is a prerequisite for colonization and further infection. The main adhesins of the emerging sexually transmitted pathogen Mycoplasma genitalium, P140 and P110, interact to form a Nap complex anchored to the cell membrane. Herein, we present the crystal structures of the extracellular region of the virulence factor P110 (916 residues) unliganded and in complex with sialic acid oligosaccharides. P110 interacts only with the neuraminic acid moiety of the oligosaccharides and experiments with human cells demonstrate that these interactions are essential for mycoplasma cytadherence. Additionally, structural information provides a deep insight of the P110 antigenic regions undergoing programmed variation to evade the host immune response. These results enlighten the interplay of M. genitalium with human target cells, offering new strategies to control mycoplasma infections.

PubMed: 30367053
DOI: 10.1038/s41467-018-06963-y

実験手法

X-RAY DIFFRACTION (2.4 Å)