Crystallization and Crystallographic Analysis of a Bradyrhizobium Elkanii USDA94 Haloalkane Dehalogenase Variant with an Eliminated Halide-Binding Site
The result's identifiers
Result code in 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>
Alternative codes found
RIV/61388971:_____/19:00508541 RIV/00216224:14310/19:00108205 RIV/00159816:_____/19:00072506
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
Crystallization and Crystallographic Analysis of a Bradyrhizobium Elkanii USDA94 Haloalkane Dehalogenase Variant with an Eliminated Halide-Binding Site
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10403 - Physical chemistry
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Crystals
ISSN
2073-4352
e-ISSN
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Volume of the periodical
9
Issue of the periodical within the volume
7
Country of publishing house
CH - SWITZERLAND
Number of pages
12
Pages from-to
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UT code for WoS article
000482052800024
EID of the result in the Scopus database
2-s2.0-85071098152