1USH

X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site.

(1999) Nat Struct Biol 6: 448-453

• PubMed: 10331872 Search on PubMed
• DOI: https://doi.org/10.1038/8253
• Primary Citation of Related Structures:  
  1USH, 2USH


• PubMed Abstract: 
  

  The crystal structure of 5'-nucleotidase (5'-NT) from E. coli, also known as UDP-sugar hydrolase, has been determined at 1.7 A resolution. Two zinc ions are present in the active site, which is located in a cleft between two domains. The dimetal center and a catalytic Asp-His dyad are the main players in the catalytic mechanism. Structure-based sequence comparisons show that the structure also provides a model for animal 5'-NTs, which together with other ectonucleotidases terminate the action of nucleotides as extracellular signaling substances in the nervous system.

   View More

---

Organizational Affiliation: 

Institut für Kristallographie, Abteilung Saenger, Freie Universit?t Berlin, Germany.