Crystal structure of native α-l-rhamnosidase from Aspergillus terreus

Petr Pachl, Jana Škerlová, Daniela Šimčíková, Michael Kotik, Alena Křenková, Pavel Mader, Jiří Brynda, Jana Kapešová, Vladimír Křen, Zbyszek Otwinowski, Pavlína Řezáčová

Research output: Contribution to journalArticlepeer-review

16 Scopus citations


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 languageEnglish (US)
Pages (from-to)1078-1084
Number of pages7
JournalActa Crystallographica Section D: Structural Biology
Issue number11
StatePublished - Nov 2018


  • Aspergillus terreus
  • carbohydrate biotechnology
  • glycosyl hydrolase
  • sulfur SAD
  • α-l-rhamnosidase

ASJC Scopus subject areas

  • Structural Biology


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