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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.
Acta Crystallographica Section F – Wiley
Published: Sep 1, 2010
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