4V1X

The structure of the hexameric atrazine chlorohydrolase, AtzA

Summary for 4V1X

• Entry DOI: 10.2210/pdb4v1x/pdb
• Related: 4V1Y
• Descriptor: ATRAZINE CHLOROHYDROLASE, FE (III) ION, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• Functional Keywords: hydrolase, bioremediation, protein evolution
• Biological source: PSEUDOMONAS SP. ADP
• Cellular location: Cytoplasm : P72156
• Total number of polymer chains: 6
• Total formula weight: 329316.28

Authors

Peat, T.S.,Newman, J.,Balotra, S.,Lucent, D.,Warden, A.C.,Scott, C. (deposition date: 2014-10-04, release date: 2015-03-11, Last modification date: 2024-05-08)

Primary citation

Peat, T.S.,Newman, J.,Balotra, S.,Lucent, D.,Warden, A.C.,Scott, C.
The Structure of the Hexameric Atrazine Chlorohydrolase Atza.
Acta Crystallogr.,Sect.D, 71:710-, 2015

PubMed 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.

PubMed: 25760618
DOI: 10.1107/S1399004715000619

Experimental method

X-RAY DIFFRACTION (2.2 Å)