The structure of a family GH25 lysozyme from Aspergillus fumigatus

Korczynska, Justyna E., Danielsen, Steffen, Schagerlöf, Ulrika , Turkenburg, Johan P., Davies, Gideon J., 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

Full content URL: http://dx.doi.org/10.1107/S1744309110025601

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Item Type:Article
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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.

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
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ID Code:6124
Deposited On:08 Sep 2012 06:52

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