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

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5 Scopus citations

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 languageEnglish (US)
Pages (from-to)1078-1084
Number of pages7
JournalActa Crystallographica Section D: Structural Biology
Volume74
Issue number11
DOIs
StatePublished - Nov 1 2018

Keywords

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

ASJC Scopus subject areas

  • Structural Biology

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    Pachl, P., Škerlová, J., Šimčíková, D., Kotik, M., Křenková, A., Mader, P., Brynda, J., Kapešová, J., Křen, V., Otwinowski, Z., & Řezáčová, P. (2018). Crystal structure of native α-l-rhamnosidase from Aspergillus terreus. Acta Crystallographica Section D: Structural Biology, 74(11), 1078-1084. https://doi.org/10.1107/S2059798318013049