Structural and molecular insights into a bifunctional glycoside hydrolase 30 xylanase specific to glucuronoxylan.
In: Biotechnology & Bioengineering, Jg. 121 (2024-07-01), Heft 7, S. 2067-2078
Online
academicJournal
Zugriff:
Glycoside hydrolase (GH) 30 family xylanases are enzymes of biotechnological interest due to their capacity to degrade recalcitrant hemicelluloses, such as glucuronoxylan (GX). This study focuses on a subfamily 7 GH30, TtXyn30A from Thermothelomyces thermophilus, which acts on GX in an "endo" and "exo" mode, releasing methyl‐glucuronic acid branched xylooligosaccharides (XOs) and xylobiose, respectively. The crystal structure of inactive TtXyn30A in complex with 23‐(4‐O‐methyl‐α‐D‐glucuronosyl)‐xylotriose (UXX), along with biochemical analyses, corroborate the implication of E233, previously identified as alternative catalytic residue, in the hydrolysis of decorated xylan. At the −1 subsite, the xylose adopts a distorted conformation, indicative of the Michaelis complex of TtXyn30AEE with UXX trapped in the semi‐functional active site. The most significant structural rearrangements upon substrate binding are observed at residues W127 and E233. The structures with neutral XOs, representing the "exo" function, clearly show the nonspecific binding at aglycon subsites, contrary to glycon sites, where the xylose molecules are accommodated via multiple interactions. Last, an unproductive ligand binding site is found at the interface between the catalytic and the secondary β‐domain which is present in all GH30 enzymes. These findings improve current understanding of the mechanism of bifunctional GH30s, with potential applications in the field of enzyme engineering. [ABSTRACT FROM AUTHOR]
Copyright of Biotechnology & Bioengineering is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Titel: |
Structural and molecular insights into a bifunctional glycoside hydrolase 30 xylanase specific to glucuronoxylan.
|
---|---|
Autor/in / Beteiligte Person: | Pentari, Christina ; Kosinas, Christos ; Nikolaivits, Efstratios ; Dimarogona, Maria ; Topakas, Evangelos |
Link: | |
Zeitschrift: | Biotechnology & Bioengineering, Jg. 121 (2024-07-01), Heft 7, S. 2067-2078 |
Veröffentlichung: | 2024 |
Medientyp: | academicJournal |
ISSN: | 0006-3592 (print) |
DOI: | 10.1002/bit.28731 |
Sonstiges: |
|