The structure of a family GH25 lysozyme from Aspergillus fumigatus

Korczynska, Justyna E. and Danielsen, Steffen and Schagerlöf, Ulrika and Turkenburg, Johan P. and Davies, Gideon J. and Wilson, Keith S. and Taylor, Edward J. (2010) The structure of a family GH25 lysozyme from Aspergillus fumigatus. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66 (9). pp. 973-977. ISSN 1744-3091

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Official URL: http://dx.doi.org/10.1107/S1744309110025601

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.

Item Type:Article
Additional Information: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.
Keywords:fungal GH25, peptidoglycan cleavage, lysins, lysozomes
Subjects:C Biological Sciences > C790 Molecular Biology, Biophysics and Biochemistry not elsewhere classified
Divisions:College of Science > School of Life Sciences
ID Code:6124
Deposited By: Bev Jones
Deposited On:08 Sep 2012 06:52
Last Modified:08 Sep 2012 06:52

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