Crystallographic analysis of 1,2,3-trichloropropane biodegradation by the haloalkane dehalogenase DhaA31

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F14%3A43886872" target="_blank" >RIV/60076658:12310/14:43886872 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60076658:12520/14:43886872

Výsledek na webu

<a href="http://loschmidt.chemi.muni.cz/peg/wp-content/uploads/2014/02/acta14.pdf" target="_blank" >http://loschmidt.chemi.muni.cz/peg/wp-content/uploads/2014/02/acta14.pdf</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 the haloalkane dehalogenase DhaA31

Popis výsledku v původním jazyce

Haloalkane dehalogenases catalyze the hydrolytic cleavage of carbon-halogen bonds, which is a key step in the 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, the 1.31 angstrom resolution crystal structure of substrate-free DhaA31, the 1.26 angstrom resolution structure of DhaA31 in complex with TCP and the 1.95 angstrom resolution structure of wild-type DhaA are reported. Crystals of the enzyme-substrate complex were successfully obtained by adding volatile TCP to the reservoirafter crystallization at pH 6.5 and room temperature. Comparison of the substrate-free structure with that of the DhaA31 enzyme-substrate complex reveals that the nucleophilic Asp106 changes its conformation from an inactive to an active

Název v anglickém jazyce

Crystallographic analysis of 1,2,3-trichloropropane biodegradation by the haloalkane dehalogenase DhaA31

Popis výsledku anglicky

Haloalkane dehalogenases catalyze the hydrolytic cleavage of carbon-halogen bonds, which is a key step in the 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, the 1.31 angstrom resolution crystal structure of substrate-free DhaA31, the 1.26 angstrom resolution structure of DhaA31 in complex with TCP and the 1.95 angstrom resolution structure of wild-type DhaA are reported. Crystals of the enzyme-substrate complex were successfully obtained by adding volatile TCP to the reservoirafter crystallization at pH 6.5 and room temperature. Comparison of the substrate-free structure with that of the DhaA31 enzyme-substrate complex reveals that the nucleophilic Asp106 changes its conformation from an inactive to an active

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2014

Kód důvěrnosti údajů

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

Název periodika

Acta Crystallographica Section D - Biological Crystallography

ISSN

1399-0047

e-ISSN

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Svazek periodika

70

Číslo periodika v rámci svazku

Neuveden

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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