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

Nat Struct Biol. 1999 May;6(5):448-53. doi: 10.1038/8253.

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • 5'-Nucleotidase / chemistry*
  • 5'-Nucleotidase / metabolism
  • Amino Acid Sequence
  • Animals
  • Aspartic Acid / chemistry
  • Aspartic Acid / metabolism
  • Binding Sites
  • Catalysis
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / enzymology*
  • Histidine / chemistry
  • Histidine / metabolism
  • Humans
  • Ligands
  • Models, Molecular
  • Molecular Sequence Data
  • Phosphoric Monoester Hydrolases / chemistry
  • Protein Conformation
  • Protein Structure, Secondary
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Zinc / metabolism*

Substances

  • Ligands
  • Aspartic Acid
  • Histidine
  • Phosphoric Monoester Hydrolases
  • 5'-Nucleotidase
  • Zinc

Associated data

  • PDB/1USH
  • PDB/2USH