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PDBsum entry 6tql

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protein ligands Protein-protein interface(s) links
Structural protein PDB id
6tql

 

 

 

 

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Contents
Protein chains
293 a.a.
141 a.a.
153 a.a.
Ligands
NAG-NAG ×2
NAG-NAG-BMA-MAN-
NAG-GAL-NAG-MAN-
NAG-NAG
NAG-NAG-BMA-MAN-
NAG-NAG-MAN-NAG
NAG ×2
PDB id:
6tql
Name: Structural protein
Title: Cryo-em of elastase-treated human uromodulin (umod)/tamm-horsfall protein (thp) filament
Structure: Uromodulin. Chain: a, b, c. Synonym: tamm-horsfall urinary glycoprotein,thp
Source: Homo sapiens. Human. Organism_taxid: 9606
Authors: A.Stsiapanava,C.Xu,M.Carroni,B.Wu,L.Jovine
Key ref: A.Stsiapanava et al. (2020). Cryo-EM structure of native human uromodulin, a zona pellucida module polymer. EMBO J, 39, e106807. PubMed id: 33196145 DOI: 10.15252/embj.2020106807
Date:
16-Dec-19     Release date:   04-Nov-20    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P07911  (UROM_HUMAN) -  Uromodulin from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
640 a.a.
293 a.a.
Protein chain
Pfam   ArchSchema ?
P07911  (UROM_HUMAN) -  Uromodulin from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
640 a.a.
141 a.a.
Protein chain
Pfam   ArchSchema ?
P07911  (UROM_HUMAN) -  Uromodulin from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
640 a.a.
153 a.a.
Key:    PfamA domain  Secondary structure

 

 
DOI no: 10.15252/embj.2020106807 EMBO J 39:e106807 (2020)
PubMed id: 33196145  
 
 
Cryo-EM structure of native human uromodulin, a zona pellucida module polymer.
A.Stsiapanava, C.Xu, M.Brunati, S.Zamora-Caballero, C.Schaeffer, M.Bokhove, L.Han, H.Hebert, M.Carroni, S.Yasumasu, L.Rampoldi, B.Wu, L.Jovine.
 
  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.
 

 

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