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Title: Structure of the Cyanuric Acid Hydrolase TrzD Reveals Product Exit Channel

Abstract

Cyanuric acid hydrolases are of industrial importance because of their use in aquatic recreational facilities to remove cyanuric acid, a stabilizer for the chlorine. Degradation of excess cyanuric acid is necessary to maintain chlorine disinfection in the waters. Cyanuric acid hydrolase opens the cyanuric acid ring hydrolytically and subsequent decarboxylation produces carbon dioxide and biuret. In the present study, we report the X-ray structure of TrzD, a cyanuric acid hydrolase from Acidovorax citrulli. The crystal structure at 2.19 Å resolution shows a large displacement of the catalytic lysine (Lys163) in domain 2 away from the active site core, whereas the two other active site lysines from the two other domains are not able to move. The lysine displacement is proposed here to open up a channel for product release. Consistent with that, the structure also showed two molecules of the co-product, carbon dioxide, one in the active site and another trapped in the proposed exit channel. Previous data indicated that the domain 2 lysine residue plays a role in activating an adjacent serine residue carrying out nucleophilic attack, opening the cyanuric acid ring, and the mobile lysine guides products through the exit channel.

Authors:
; ; ;
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
USDOE; National Science Foundation (NSF)
OSTI Identifier:
1349927
Resource Type:
Journal Article
Journal Name:
Scientific Reports
Additional Journal Information:
Journal Volume: 7; Journal Issue: 02, 2017; Journal ID: ISSN 2045-2322
Publisher:
Nature Publishing Group
Country of Publication:
United States
Language:
ENGLISH
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY

Citation Formats

Bera, Asim K., Aukema, Kelly G., Elias, Mikael, and Wackett, Lawrence P. Structure of the Cyanuric Acid Hydrolase TrzD Reveals Product Exit Channel. United States: N. p., 2017. Web. doi:10.1038/srep45277.
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Bera, Asim K., Aukema, Kelly G., Elias, Mikael, & Wackett, Lawrence P. Structure of the Cyanuric Acid Hydrolase TrzD Reveals Product Exit Channel. United States. doi:10.1038/srep45277.
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Bera, Asim K., Aukema, Kelly G., Elias, Mikael, and Wackett, Lawrence P. Mon . "Structure of the Cyanuric Acid Hydrolase TrzD Reveals Product Exit Channel". United States. doi:10.1038/srep45277.
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@article{osti_1349927,
title = {Structure of the Cyanuric Acid Hydrolase TrzD Reveals Product Exit Channel},
author = {Bera, Asim K. and Aukema, Kelly G. and Elias, Mikael and Wackett, Lawrence P.},
abstractNote = {Cyanuric acid hydrolases are of industrial importance because of their use in aquatic recreational facilities to remove cyanuric acid, a stabilizer for the chlorine. Degradation of excess cyanuric acid is necessary to maintain chlorine disinfection in the waters. Cyanuric acid hydrolase opens the cyanuric acid ring hydrolytically and subsequent decarboxylation produces carbon dioxide and biuret. In the present study, we report the X-ray structure of TrzD, a cyanuric acid hydrolase from Acidovorax citrulli. The crystal structure at 2.19 Å resolution shows a large displacement of the catalytic lysine (Lys163) in domain 2 away from the active site core, whereas the two other active site lysines from the two other domains are not able to move. The lysine displacement is proposed here to open up a channel for product release. Consistent with that, the structure also showed two molecules of the co-product, carbon dioxide, one in the active site and another trapped in the proposed exit channel. Previous data indicated that the domain 2 lysine residue plays a role in activating an adjacent serine residue carrying out nucleophilic attack, opening the cyanuric acid ring, and the mobile lysine guides products through the exit channel.},
doi = {10.1038/srep45277},
journal = {Scientific Reports},
issn = {2045-2322},
number = 02, 2017,
volume = 7,
place = {United States},
year = {2017},
month = {3}
}
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Journal Article:
DOI:  10.1038/srep45277
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