Crystal structure of native beta-N-acetylhexosaminidase isolated from Aspergillus oryzae sheds light onto its substrate specificity, high stability, and regulation by propeptide

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F18%3A10374397" target="_blank" >RIV/00216208:11310/18:10374397 - isvavai.cz</a>

Alternative codes found

RIV/61388971:_____/18:00491223 RIV/68378050:_____/18:00491223 RIV/61388963:_____/18:00489879 RIV/00216208:11320/18:10374397

Result on the web

<a href="https://doi.org/10.1111/febs.14360" target="_blank" >https://doi.org/10.1111/febs.14360</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1111/febs.14360" target="_blank" >10.1111/febs.14360</a>

Result language

angličtina

Original language name

Crystal structure of native beta-N-acetylhexosaminidase isolated from Aspergillus oryzae sheds light onto its substrate specificity, high stability, and regulation by propeptide

Original language description

beta-N-acetylhexosaminidase from the fungus Aspergillus oryzae is a secreted extracellular enzyme that cleaves chitobiose into constituent monosaccharides. It belongs to the GH 20 glycoside hydrolase family and consists of two N-glycosylated catalytic cores noncovalently associated with two 10-kDa O-glycosylated propeptides. We used X-ray diffraction and mass spectrometry to determine the structure of A. oryzae beta-N-acetylhexosaminidase isolated from its natural source. The three-dimensional structure determined and refined to a resolution of 2.3 angstrom revealed that this enzyme is active as a uniquely tight dimeric assembly further stabilized by N-and O-glycosylation. The propeptide from one subunit forms extensive noncovalent interactions with the catalytic core of the second subunit in the dimer, and this chain swap suggests the distinctive structural mechanism of the enzyme&apos;s activation. Unique structural features of beta-N-acetylhexosaminidase from A. oryzae define a very stable and robust framework suitable for biotechnological applications. The crystal structure reported here provides structural insights into the enzyme architecture as well as the detailed configuration of the active site. These insights can be applied to rational enzyme engineering. Database Structural data are available in the PDB database under the accession number 5OAR.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10608 - Biochemistry and molecular biology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2018

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

FEBS Journal

ISSN

1742-464X

e-ISSN

—

Volume of the periodical

285

Issue of the periodical within the volume

3

Country of publishing house

GB - UNITED KINGDOM

Number of pages

19

Pages from-to

580-598

UT code for WoS article

000424168600011

EID of the result in the Scopus database

2-s2.0-85039557159