All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

The tetrameric structure of the novel haloalkane dehalogenase DpaA from Paraglaciecola agarilytica NO2

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F21%3A43903272" target="_blank" >RIV/60076658:12310/21:43903272 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216224:14310/21:00119187 RIV/00159816:_____/21:00075110 RIV/68407700:21340/21:00351032

  • Result on the web

    <a href="https://scripts.iucr.org/cgi-bin/paper?S2059798321000486" target="_blank" >https://scripts.iucr.org/cgi-bin/paper?S2059798321000486</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1107/S2059798321000486" target="_blank" >10.1107/S2059798321000486</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    The tetrameric structure of the novel haloalkane dehalogenase DpaA from Paraglaciecola agarilytica NO2

  • Original language description

    Haloalkane dehalogenases (EC 3.8.1.5) are microbial enzymes that catalyse the hydrolytic conversion of halogenated compounds, resulting in a halide ion, a proton and an alcohol. These enzymes are used in industrial biocatalysis, bioremediation and biosensing of environmental pollutants or for molecular tagging in cell biology. The novel haloalkane dehalogenase DpaA described here was isolated from the psychrophilic and halophilic bacterium Paraglaciecola agarilytica NO2, which was found in marine sediment collected from the East Sea near Korea. Gel-filtration experiments and size-exclusion chromatography provided information about the dimeric composition of the enzyme in solution. The DpaA enzyme was crystallized using the sitting-drop vapour-diffusion method, yielding rod-like crystals that diffracted X-rays to 2.0 angstrom resolution. Diffraction data analysis revealed a case of merohedral twinning, and subsequent structure modelling and refinement resulted in a tetrameric model of DpaA, highlighting an uncommon multimeric nature for a protein belonging to haloalkane dehalogenase subfamily I.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

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)<br>S - Specificky vyzkum na vysokych skolach

Others

  • Publication year

    2021

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Acta crystallographica. Section D - Structural Biology

  • ISSN

    2059-7983

  • e-ISSN

  • Volume of the periodical

    77

  • Issue of the periodical within the volume

    MAR 1 2021

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    10

  • Pages from-to

    347-356

  • UT code for WoS article

    000625172500009

  • EID of the result in the Scopus database

    2-s2.0-85102070813