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Crystal structure of native α-L-rhamnosidase from Aspergillus terreus
P. Pachl, J. Škerlová, D. Šimčíková, M. Kotik, A. Křenková, P. Mader, J. Brynda, J. Kapešová, V. Křen, Z. Otwinowski, P. Řezáčová,
Language English Country United States
Document type Journal Article
- MeSH
- Aspergillus enzymology MeSH
- Glycoside Hydrolases chemistry metabolism MeSH
- Glycosylation MeSH
- Catalytic Domain MeSH
- Protein Conformation * MeSH
- Crystallography, X-Ray MeSH
- Models, Molecular MeSH
- Publication type
- Journal Article MeSH
α-L-Rhamnosidases cleave terminal nonreducing α-L-rhamnosyl residues from many natural rhamnoglycosides. This makes them catalysts of interest for various biotechnological applications. The X-ray structure of the GH78 family α-L-rhamnosidase from Aspergillus terreus has been determined at 1.38 Å 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, the α-L-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.
Institute of Microbiology The Czech Academy of Sciences Vídeňská 1083 14220 Prague 4 Czech Republic
UT Southwestern Medical Center 5323 Harry Hines Boulevard Dallas Texas USA
References provided by Crossref.org
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