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Publication Abstract from PubMed

alpha-L-Rhamnosidases cleave terminal nonreducing alpha-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 alpha-L-rhamnosidase from Aspergillus terreus has been determined at 1.38 A 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 alpha-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.

Crystal structure of native alpha-L-rhamnosidase from Aspergillus terreus.,Pachl P, Skerlova J, Simcikova D, Kotik M, Krenkova A, Mader P, Brynda J, Kapesova J, Kren V, Otwinowski Z, Rezacova P Acta Crystallogr D Struct Biol. 2018 Nov 1;74(Pt 11):1078-1084. doi:, 10.1107/S2059798318013049. Epub 2018 Oct 29. PMID:30387766^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.