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The structure of a family GH25 lysozyme from Aspergillus fumigatus

The structure of a family GH25 lysozyme from Aspergillus fumigatus Lysins are important biomolecules which cleave the bacterial cell‐wall polymer peptidoglycan. They are finding increasing commercial and medical application. In order to gain an insight into the mechanism by which these enzymes operate, the X‐ray structure of a CAZy family GH25 `lysozyme' from Aspergillus fumigatus was determined. This is the first fungal structure from the family and reveals a modified α/β‐barrel‐like fold in which an eight‐stranded β‐barrel is flanked by three α‐helices. The active site lies toward the bottom of a negatively charged pocket and its layout has much in common with other solved members of the GH25 and related GH families. A conserved active‐site DXE motif may be implicated in catalysis, lending further weight to the argument that this glycoside hydrolase family operates via a `substrate‐assisted' catalytic mechanism. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

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References (36)

Publisher
Wiley
Copyright
International Union of Crystallography, 2010
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309110025601
pmid
20823508
Publisher site
See Article on Publisher Site

Abstract

Lysins are important biomolecules which cleave the bacterial cell‐wall polymer peptidoglycan. They are finding increasing commercial and medical application. In order to gain an insight into the mechanism by which these enzymes operate, the X‐ray structure of a CAZy family GH25 `lysozyme' from Aspergillus fumigatus was determined. This is the first fungal structure from the family and reveals a modified α/β‐barrel‐like fold in which an eight‐stranded β‐barrel is flanked by three α‐helices. The active site lies toward the bottom of a negatively charged pocket and its layout has much in common with other solved members of the GH25 and related GH families. A conserved active‐site DXE motif may be implicated in catalysis, lending further weight to the argument that this glycoside hydrolase family operates via a `substrate‐assisted' catalytic mechanism.

Journal

Acta Crystallographica Section FWiley

Published: Sep 1, 2010

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