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Crystal structure of nativel-rhamnosidase from Aspergillus terreus

  1. 1.
    0501870 - ÚMG 2019 RIV GB eng J - Článek v odborném periodiku
    Pachl, P. - Škerlová, J. - Šimčíková, D. - Kotik, M. - Krenkova, A. - Mader, Pavel - Brynda, Jiří - Kapešová, J. - Křen, V. - Otwinowski, Z. - Řezáčová, Pavlína
    Crystal structure of nativel-rhamnosidase from Aspergillus terreus.
    Acta Crystallographica Section D-Structural Biology. Roč. 74, November (2018), s. 1078-1084. ISSN 2059-7983. E-ISSN 2059-7983
    Grant CEP: GA MŠMT(CZ) LTC18041
    Institucionální podpora: RVO:68378050 ; RVO:61388971
    Klíčová slova: glycosyl hydrolase * carbohydrate biotechnology * sulfur SAD * alpha-l-rhamnosidase * Aspergillus terreus
    Obor OECD: Biochemistry and molecular biology
    Impakt faktor: 3.227, rok: 2018

    alpha-l-Rhamnosidases cleave terminal nonreducingl-rhamnosyl residues from many natural rhamnoglycosides. This makes them catalysts of interest for various biotechnological applications. The X-ray structure of the GH78 familyl-rhamnosidase from Aspergillus terreus has been determined at 1.38 angstrom resolution using the sulfur single-wavelength anomalous dispersion phasing method. The protein was isolated from its natural source in the native glycosylated form, and the active site contained a glucose molecule, probably from the growth medium. In addition to its catalytic domain, thel-rhamnosidase from A.terreus contains four accessory domains of unknown function. The structural data suggest that two of these accessory domains, E and F, might play a role in stabilizing the aglycon portion of the bound substrate.
    Trvalý link: http://hdl.handle.net/11104/0293852

     
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