The structure of the hexameric atrazine chlorohydrolase AtzA

Acta Crystallogr D Biol Crystallogr. 2015 Mar;71(Pt 3):710-20. doi: 10.1107/S1399004715000619. Epub 2015 Feb 26.

Abstract

Atrazine chlorohydrolase (AtzA) was discovered and purified in the early 1990s from soil that had been exposed to the widely used herbicide atrazine. It was subsequently found that this enzyme catalyzes the first and necessary step in the breakdown of atrazine by the soil organism Pseudomonas sp. strain ADP. Although it has taken 20 years, a crystal structure of the full hexameric form of AtzA has now been obtained. AtzA is less well adapted to its physiological role (i.e. atrazine dechlorination) than the alternative metal-dependent atrazine chlorohydrolase (TrzN), with a substrate-binding pocket that is under considerable strain and for which the substrate is a poor fit.

Keywords: atrazine chlorohydrolase.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Crystallography, X-Ray
  • Hydrolases / chemistry*
  • Protein Structure, Tertiary
  • Pseudomonas / enzymology*
  • Soil Microbiology*

Substances

  • Bacterial Proteins
  • Hydrolases
  • atrazine chlorohydrolase