Crystallization and Crystallographic Analysis of a Bradyrhizobium Elkanii USDA94 Haloalkane Dehalogenase Variant with an Eliminated Halide-Binding Site

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F19%3A43899512" target="_blank" >RIV/60076658:12310/19:43899512 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388971:_____/19:00508541 RIV/00216224:14310/19:00108205 RIV/00159816:_____/19:00072506

Výsledek na webu

<a href="http://file:///C:/Users/jmaxerova/Desktop/crystals-09-00375.pdf" target="_blank" >http://file:///C:/Users/jmaxerova/Desktop/crystals-09-00375.pdf</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3390/cryst9070375" target="_blank" >10.3390/cryst9070375</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Crystallization and Crystallographic Analysis of a Bradyrhizobium Elkanii USDA94 Haloalkane Dehalogenase Variant with an Eliminated Halide-Binding Site

Popis výsledku v původním jazyce

Haloalkane dehalogenases are a very important class of microbial enzymes for environmental detoxification of halogenated pollutants, for biocatalysis, biosensing and molecular tagging. The double mutant (Ile44Leu + Gln102His) of the haloalkane dehalogenase DbeA from Bradyrhizobium elkanii USDA94 (DbeA Delta Cl) was constructed to study the role of the second halide-binding site previously discovered in the wild-type structure. The variant is less active, less stable in the presence of chloride ions and exhibits significantly altered substrate specificity when compared with the DbeAwt. DbeA Delta Cl was crystallized using the sitting-drop vapour-diffusion procedure with further optimization by the random microseeding technique. The crystal structure of the DbeA Delta Cl has been determined and refined to the 1.4 angstrom resolution. The DbeA Delta Cl crystals belong to monoclinic space group C121. The DbeA Delta Cl molecular structure was characterized and compared with five known haloalkane dehalogenases selected from the Protein Data Bank.

Název v anglickém jazyce

Crystallization and Crystallographic Analysis of a Bradyrhizobium Elkanii USDA94 Haloalkane Dehalogenase Variant with an Eliminated Halide-Binding Site

Popis výsledku anglicky

Haloalkane dehalogenases are a very important class of microbial enzymes for environmental detoxification of halogenated pollutants, for biocatalysis, biosensing and molecular tagging. The double mutant (Ile44Leu + Gln102His) of the haloalkane dehalogenase DbeA from Bradyrhizobium elkanii USDA94 (DbeA Delta Cl) was constructed to study the role of the second halide-binding site previously discovered in the wild-type structure. The variant is less active, less stable in the presence of chloride ions and exhibits significantly altered substrate specificity when compared with the DbeAwt. DbeA Delta Cl was crystallized using the sitting-drop vapour-diffusion procedure with further optimization by the random microseeding technique. The crystal structure of the DbeA Delta Cl has been determined and refined to the 1.4 angstrom resolution. The DbeA Delta Cl crystals belong to monoclinic space group C121. The DbeA Delta Cl molecular structure was characterized and compared with five known haloalkane dehalogenases selected from the Protein Data Bank.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10403 - Physical chemistry

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)

Rok uplatnění

2019

Kód důvěrnosti údajů

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

Název periodika

Crystals

ISSN

2073-4352

e-ISSN

—

Svazek periodika

9

Číslo periodika v rámci svazku

7

Stát vydavatele periodika

CH - Švýcarská konfederace

Počet stran výsledku

12

Strana od-do

—

Kód UT WoS článku

000482052800024

EID výsledku v databázi Scopus

2-s2.0-85071098152