6TQK

Cryo-EM of native human uromodulin (UMOD)/Tamm-Horsfall protein (THP) filament.

6TQK の概要

• エントリーDOI: 10.2210/pdb6tqk/pdb
• 関連するPDBエントリー: 3NK4 4WRN 6TQL
• EMDBエントリー: 10553 10554
• 分子名称: Uromodulin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)]alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: zp module, zp domain, zp-n domain, zp-c domain, interdomain linker, egf domain, extracellular matrix, glycoprotein, n-glycan, structural protein, protein filament, protein polymerization
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 188746.36

構造登録者

Stsiapanava, A.,Xu, C.,Carroni, M.,Wu, B.,Jovine, L. (登録日: 2019-12-16, 公開日: 2020-11-04, 最終更新日: 2024-10-09)

主引用文献

Stsiapanava, A.,Xu, C.,Brunati, M.,Zamora-Caballero, S.,Schaeffer, C.,Bokhove, M.,Han, L.,Hebert, H.,Carroni, M.,Yasumasu, S.,Rampoldi, L.,Wu, B.,Jovine, L.
Cryo-EM structure of native human uromodulin, a zona pellucida module polymer.
Embo J., 39:e106807-e106807, 2020

PubMed Abstract: Assembly of extracellular filaments and matrices mediating fundamental biological processes such as morphogenesis, hearing, fertilization, and antibacterial defense is driven by a ubiquitous polymerization module known as zona pellucida (ZP) "domain". Despite the conservation of this element from hydra to humans, no detailed information is available on the filamentous conformation of any ZP module protein. Here, we report a cryo-electron microscopy study of uromodulin (UMOD)/Tamm-Horsfall protein, the most abundant protein in human urine and an archetypal ZP module-containing molecule, in its mature homopolymeric state. UMOD forms a one-start helix with an unprecedented 180-degree twist between subunits enfolded by interdomain linkers that have completely reorganized as a result of propeptide dissociation. Lateral interaction between filaments in the urine generates sheets exposing a checkerboard of binding sites to capture uropathogenic bacteria, and UMOD-based models of heteromeric vertebrate egg coat filaments identify a common sperm-binding region at the interface between subunits.

PubMed: 33196145
DOI: 10.15252/embj.2020106807

実験手法

ELECTRON MICROSCOPY (3.35 Å)