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Structural Properties and Electrostatics of Cold-active beta-Galactosidase

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F07%3A00019134" target="_blank" >RIV/60461373:22330/07:00019134 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Structural Properties and Electrostatics of Cold-active beta-Galactosidase

  • Original language description

    Arthrobacter sp. C2-2, a soil bacteria found on an island near Antarctica, belongs to psychrotrophic, i.e. cold tolerant, microorganisms. Structure of its betagalactosidase (hydrolase cleaving lactose into galactose and glucose), iso-enzyme C-2-2-1, wassolved up to 1.9 ? resolution. The beta-galactosidase belongs to glycosyl hydrolase structural family 2 and has 30% sequence identity with Escherichia coli beta-galactosidase. In spite of the chain similarity, both enzymes differ in their oligomerizationstates. Escherichia coli beta-galactosidase is known to be active only in the form of tetramers, while the cold-active Arthrobacter sp. C2-2 beta-galactosidase forms compact hexamers with active sites oriented into an internal cavity, connected by threetypes of channels with exterior solvent. Additionally, sequence differences between both enzymes exist in the active site.

  • Czech name

    Strukturní vlastnosti a elektrostatika chladově-aktivní beta-galaktosidasy

  • Czech description

    Strukturní vlastnosti a elektrostatika chladově-aktivní beta-galaktosidasy byla presentována

Classification

  • Type

    D - Article in proceedings

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/KJB500500512" target="_blank" >KJB500500512: Structural studies of beta-galactosidase from psychrotrophic microorganisms; analysis of biologically and technologically significant complexes</a><br>

  • Continuities

    Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2007

  • Confidentiality

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

Data specific for result type

  • Article name in the collection

    Acta Crystallogr., Sect.A: Cryst.Phys.,Diffr.,Theor.Gen.Crystallogr.

  • ISBN

  • ISSN

    0567-7394

  • e-ISSN

  • Number of pages

    2

  • Pages from-to

    "s125"-"s126"

  • Publisher name

    IUCr, International Union of Crystallography

  • Place of publication

    Chester

  • Event location

  • Event date

  • Type of event by nationality

  • UT code for WoS article