The structure of the hexameric atrazine chlorohydrolase AtzA

T. S. Peat, J. Newman, S. Balotra, D. Lucent, A. C. Warden, C. Scott*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

18 Citations (Scopus)
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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.

Original languageEnglish
Pages (from-to)710-720
Number of pages11
JournalActa Crystallographica Section D: Biological Crystallography
Publication statusPublished - 1 Mar 2015
Externally publishedYes

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  • atrazine chlorohydrolase


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