2QIH

Crystal structure of 527-665 fragment of UspA1 protein from Moraxella catarrhalis

2QIH の概要

• エントリーDOI: 10.2210/pdb2qih/pdb
• 分子名称: protein UspA1, PHOSPHATE ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: trimeric; parallel alpha-helical coiled-coil, cell adhesion
• 由来する生物種: Moraxella catarrhalis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34792.64

構造登録者

Conners, R.,Brady, R.L. (登録日: 2007-07-04, 公開日: 2008-05-20, 最終更新日: 2023-08-30)

主引用文献

Conners, R.,Hill, D.J.,Borodina, E.,Agnew, C.,Daniell, S.J.,Burton, N.M.,Sessions, R.B.,Clarke, A.R.,Catto, L.E.,Lammie, D.,Wess, T.,Brady, R.L.,Virji, M.
The Moraxella adhesin UspA1 binds to its human CEACAM1 receptor by a deformable trimeric coiled-coil.
Embo J., 27:1779-1789, 2008

PubMed Abstract: Moraxella catarrhalis is a ubiquitous human-specific bacterium commonly associated with upper and lower respiratory tract infections, including otitis media, sinusitis and chronic obstructive pulmonary disease. The bacterium uses an autotransporter protein UspA1 to target an important human cellular receptor carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1). Using X-ray crystallography, we show that the CEACAM1 receptor-binding region of UspA1 unusually consists of an extended, rod-like left-handed trimeric coiled-coil. Mutagenesis and binding studies of UspA1 and the N-domain of CEACAM1 have been used to delineate the interacting surfaces between ligand and receptor and guide assembly of the complex. However, solution scattering, molecular modelling and electron microscopy analyses all indicate that significant bending of the UspA1 coiled-coil stalk also occurs. This explains how UspA1 can engage CEACAM1 at a site far distant from its head group, permitting closer proximity of the respective cell surfaces during infection.

PubMed: 18497748
DOI: 10.1038/emboj.2008.101

実験手法

X-RAY DIFFRACTION (1.897 Å)