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

J. Škerlová, J. Bláha, P. Pachl, K. Hofbauerová, Z. Kukačka, P. Man, P. Pompach, P. Novák, Z. Otwinowski, J. Brynda, O. Vaněk, P. Řezáčová,

. 2018 ; 285 (3) : 580-598. [pub] 20171230

Jazyk angličtina Země Anglie, Velká Británie

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc19001037

β-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 β-N-acetylhexosaminidase isolated from its natural source. The three-dimensional structure determined and refined to a resolution of 2.3 Å 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's activation. Unique structural features of β-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. ENZYME: β-N-acetylhexosaminidase (EC 3.2.1.52).

Citace poskytuje Crossref.org

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$a Crystal structure of native β-N-acetylhexosaminidase isolated from Aspergillus oryzae sheds light onto its substrate specificity, high stability, and regulation by propeptide / $c J. Škerlová, J. Bláha, P. Pachl, K. Hofbauerová, Z. Kukačka, P. Man, P. Pompach, P. Novák, Z. Otwinowski, J. Brynda, O. Vaněk, P. Řezáčová,
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$a β-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 β-N-acetylhexosaminidase isolated from its natural source. The three-dimensional structure determined and refined to a resolution of 2.3 Å 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's activation. Unique structural features of β-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. ENZYME: β-N-acetylhexosaminidase (EC 3.2.1.52).
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$a Bláha, Jan $u Department of Biochemistry, Faculty of Science, Charles University, Prague, Czech Republic.
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$a Pachl, Petr $u Institute of Organic Chemistry and Biochemistry, The Czech Academy of Sciences, Prague, Czech Republic.
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$a Hofbauerová, Kateřina $u Institute of Microbiology, The Czech Academy of Sciences, Prague, Czech Republic. Institute of Physics, Faculty of Mathematics and Physics, Charles University, Prague, Czech Republic.
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$a Kukačka, Zdeněk $u Department of Biochemistry, Faculty of Science, Charles University, Prague, Czech Republic. Institute of Microbiology, The Czech Academy of Sciences, Prague, Czech Republic.
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$a Man, Petr $u Department of Biochemistry, Faculty of Science, Charles University, Prague, Czech Republic. Institute of Microbiology, The Czech Academy of Sciences, Prague, Czech Republic.
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$a Pompach, Petr $u Institute of Microbiology, The Czech Academy of Sciences, Prague, Czech Republic.
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$a Novák, Petr $u Department of Biochemistry, Faculty of Science, Charles University, Prague, Czech Republic. Institute of Microbiology, The Czech Academy of Sciences, Prague, Czech Republic.
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$a Otwinowski, Zbyszek $u UT Southwestern Medical Center, Dallas, TX, USA.
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$a Brynda, Jiří $u Institute of Organic Chemistry and Biochemistry, The Czech Academy of Sciences, Prague, Czech Republic. Institute of Molecular Genetics, The Czech Academy of Sciences, Prague, Czech Republic.
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$a Vaněk, Ondřej $u Department of Biochemistry, Faculty of Science, Charles University, Prague, Czech Republic.
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$a Řezáčová, Pavlína $u Institute of Organic Chemistry and Biochemistry, The Czech Academy of Sciences, Prague, Czech Republic. Institute of Molecular Genetics, The Czech Academy of Sciences, Prague, Czech Republic.
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