Abstract
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.
Original language | English (US) |
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Pages (from-to) | 1078-1084 |
Number of pages | 7 |
Journal | Acta Crystallographica Section D: Structural Biology |
Volume | 74 |
Issue number | 11 |
DOIs | |
State | Published - Nov 2018 |
Keywords
- Aspergillus terreus
- carbohydrate biotechnology
- glycosyl hydrolase
- sulfur SAD
- α-l-rhamnosidase
ASJC Scopus subject areas
- Structural Biology