Crystal structure of nativel-rhamnosidase from Aspergillus terreus

0501870 - ÚMG 2019 RIV GB eng J - Journal Article
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
R&D Projects: GA MŠMT(CZ) LTC18041
Institutional support: RVO:68378050 ; RVO:61388971
Keywords : glycosyl hydrolase * carbohydrate biotechnology * sulfur SAD * alpha-l-rhamnosidase * Aspergillus terreus
OECD category: Biochemistry and molecular biology
Impact factor: 3.227, year: 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.
Permanent Link: http://hdl.handle.net/11104/0293852