Crystallographic Analysis of 1,2,3?Trichloropropane Biodegradation by Haloalkane Dehalogenase DhaA31

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F14%3A00074213" target="_blank" >RIV/00216224:14310/14:00074213 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1107/S1399004713026254" target="_blank" >http://dx.doi.org/10.1107/S1399004713026254</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1107/S1399004713026254" target="_blank" >10.1107/S1399004713026254</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Crystallographic Analysis of 1,2,3?Trichloropropane Biodegradation by Haloalkane Dehalogenase DhaA31

Popis výsledku v původním jazyce

Haloalkane dehalogenases catalyze the hydrolytic cleavage of carbon-halogen bonds, which is a key step in aerobic mineralization of many environmental pollutants. One important pollutant is the toxic and anthropogenic compound 1,2,3-trichloropropane (TCP). Rational design was combined with saturation mutagenesis to obtain the haloalkane dehalogenase variant DhaA31, which displays an increased catalytic activity towards TCP. Here we report the 1.31 A crystal structure of substrate-free DhaA31, the 1.26 Astructure of DhaA31 in a complex with TCP, and the 1.85 A wild-type DhaA structure. Crystals of the enzyme-substrate complex were successfully obtained by adding volatile TCP to the reservoir at crystallization at room temperature and pH 6.4. Comparisonof the substrate-free structure with the DhaA31 enzyme-substrate complex reveals that the nucleophilic Asp106 changes its conformation from an inactive to an active state during the catalytic cycle.

Název v anglickém jazyce

Crystallographic Analysis of 1,2,3?Trichloropropane Biodegradation by Haloalkane Dehalogenase DhaA31

Popis výsledku anglicky

Haloalkane dehalogenases catalyze the hydrolytic cleavage of carbon-halogen bonds, which is a key step in aerobic mineralization of many environmental pollutants. One important pollutant is the toxic and anthropogenic compound 1,2,3-trichloropropane (TCP). Rational design was combined with saturation mutagenesis to obtain the haloalkane dehalogenase variant DhaA31, which displays an increased catalytic activity towards TCP. Here we report the 1.31 A crystal structure of substrate-free DhaA31, the 1.26 Astructure of DhaA31 in a complex with TCP, and the 1.85 A wild-type DhaA structure. Crystals of the enzyme-substrate complex were successfully obtained by adding volatile TCP to the reservoir at crystallization at room temperature and pH 6.4. Comparisonof the substrate-free structure with the DhaA31 enzyme-substrate complex reveals that the nucleophilic Asp106 changes its conformation from an inactive to an active state during the catalytic cycle.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GAP207%2F12%2F0775" target="_blank" >GAP207/12/0775: Strukturně-funkční vztahy haloalkan dehalogenas</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2014

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Acta Crystallographica D

ISSN

0907-4449

e-ISSN

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Svazek periodika

70

Číslo periodika v rámci svazku

february

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

9

Strana od-do

209-217

Kód UT WoS článku

000331554500001

EID výsledku v databázi Scopus

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