The structure of the hexameric atrazine chlorohydrolase AtzA

Acta Crystallographica. Section D, Biological Crystallography
T S PeatColin Scott

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.

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Citations

Mar 25, 2016·Bioscience, Biotechnology, and Biochemistry·Yuan GuoDefu Chen
May 8, 2018·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Thiau-Fu AngThean Chor Leow
Mar 11, 2018·The Journal of Biological Chemistry·Lygie EsquirolColin Scott
Apr 7, 2020·The FEBS Journal·Shelley D Copley
Nov 7, 2019·Acta Crystallographica. Section D, Structural Biology·Matthew L DennisThomas S Peat
Jun 18, 2020·Microorganisms·Justas VaitekūnasRolandas Meškys
May 3, 2020·The Journal of Biological Chemistry·Daniel S CatlinDali Liu

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Methods Mentioned

BETA
deamination
X-ray
size-exclusion chromatography

Software Mentioned

OpenEye
QuacPac
XDS
RosettaLigand
Gaussian
AIMLESS
Coot
Rosetta
Omega

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