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The structure of a family GH25 lysozyme from Aspergillus fumigatus

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JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
DatePublished - Sep 2010
Issue number9
Volume66
Number of pages5
Pages (from-to)973-977
Original languageEnglish

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 alpha/beta-barrel-like fold in which an eight-stranded beta-barrel is flanked by three alpha-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.

    Research areas

  • lysozymes, lysins, peptidoglycan cleavage, fungal GH25, PHAGE LYTIC ENZYME, CRYSTAL-STRUCTURE, BACILLUS-ANTHRACIS, CELL-WALL, RECOGNITION, ENDOLYSIN, CPL-1

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