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.
| Original language | English |
|---|---|
| Pages (from-to) | 973-977 |
| Number of pages | 5 |
| Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
| Volume | 66 |
| Issue number | 9 |
| DOIs | |
| Publication status | Published - Sept 2010 |
Keywords
- lysozymes
- lysins
- peptidoglycan cleavage
- fungal GH25
- PHAGE LYTIC ENZYME
- CRYSTAL-STRUCTURE
- BACILLUS-ANTHRACIS
- CELL-WALL
- RECOGNITION
- ENDOLYSIN
- CPL-1