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TitleThe cryo-EM structure of the human uromodulin filament core reveals a unique assembly mechanism.
Journal, issue, pagesElife, Vol. 9, Year 2020
Publish dateAug 20, 2020
AuthorsJessica J Stanisich / Dawid S Zyla / Pavel Afanasyev / Jingwei Xu / Anne Kipp / Eric Olinger / Olivier Devuyst / Martin Pilhofer / Daniel Boehringer / Rudi Glockshuber /
PubMed AbstractThe glycoprotein uromodulin (UMOD) is the most abundant protein in human urine and forms filamentous homopolymers that encapsulate and aggregate uropathogens, promoting pathogen clearance by urine ...The glycoprotein uromodulin (UMOD) is the most abundant protein in human urine and forms filamentous homopolymers that encapsulate and aggregate uropathogens, promoting pathogen clearance by urine excretion. Despite its critical role in the innate immune response against urinary tract infections, the structural basis and mechanism of UMOD polymerization remained unknown. Here, we present the cryo-EM structure of the UMOD filament core at 3.5 Å resolution, comprised of the bipartite zona pellucida (ZP) module in a helical arrangement with a rise of ~65 Å and a twist of ~180°. The immunoglobulin-like ZPN and ZPC subdomains of each monomer are separated by a long linker that interacts with the preceding ZPC and following ZPN subdomains by β-sheet complementation. The unique filament architecture suggests an assembly mechanism in which subunit incorporation could be synchronized with proteolytic cleavage of the C-terminal pro-peptide that anchors assembly-incompetent UMOD precursors to the membrane.
External linksElife / PubMed:32815518 / PubMed Central
MethodsEM (single particle)
Resolution3.5 - 4.7 Å
Structure data

11388

6zs5

6zya

EMDB-11388, PDB-6zs5:
3.5 A cryo-EM structure of human uromodulin filament core
PDB-6zya: Extended human uromodulin filament core at 3.5 A resolution
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-11471:
Extended cryo-EM map of native human uromodulin filament core at 4.7 A resolution
Method: EM (single particle) / Resolution: 4.7 Å

Source
  • homo sapiens (human)
  • Human (human)
KeywordsANTIMICROBIAL PROTEIN / Uromodulin / Umod / THP / immunoglobulin-like fold / Tamm-Horsfall protein / glycoprotein / ZP module / Zona Pellucida / fold complementation / beta-strand complementation / cryoSPARC / filament / soluble adhesion antagonist

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