7PFP
Full-length cryo-EM structure of the native human uromodulin (UMOD)/Tamm-Horsfall protein (THP) filament
Summary for 7PFP
Entry DOI | 10.2210/pdb7pfp/pdb |
Related | 4WRN 6TQK 6TQL 7P6R 7P6S 7P6T |
EMDB information | 10553 10554 13378 |
Descriptor | Uromodulin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total) |
Functional Keywords | egf domain, decoy module, beta-hairpin, d10c domain, zp module, zp domain, zp-n domain, zp-c domain, interdomain linker, extracellular matrix, glycoprotein, n-glycan, structural protein, protein filament, protein polymerization, antimicrobial protein |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 3 |
Total formula weight | 224801.05 |
Authors | Jovine, L.,Xu, C.,Stsiapanava, A.,Carroni, M.,Tunyasuvunakool, K.,Jumper, J.,Wu, B. (deposition date: 2021-08-11, release date: 2022-03-16, Last modification date: 2024-10-16) |
Primary citation | Stsiapanava, A.,Xu, C.,Nishio, S.,Han, L.,Yamakawa, N.,Carroni, M.,Tunyasuvunakool, K.,Jumper, J.,de Sanctis, D.,Wu, B.,Jovine, L. Structure of the decoy module of human glycoprotein 2 and uromodulin and its interaction with bacterial adhesin FimH. Nat.Struct.Mol.Biol., 29:190-193, 2022 Cited by PubMed Abstract: Glycoprotein 2 (GP2) and uromodulin (UMOD) filaments protect against gastrointestinal and urinary tract infections by acting as decoys for bacterial fimbrial lectin FimH. By combining AlphaFold2 predictions with X-ray crystallography and cryo-EM, we show that these proteins contain a bipartite decoy module whose new fold presents the high-mannose glycan recognized by FimH. The structure rationalizes UMOD mutations associated with kidney diseases and visualizes a key epitope implicated in cast nephropathy. PubMed: 35273390DOI: 10.1038/s41594-022-00729-3 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (6.1 Å) |
Structure validation
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