The structure of a family GH25 lysozyme from Aspergillus fumigatus.
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.
Korczynska
Justyna E
JE
Structural Biology Laboratory, Department of Chemistry, The University of York, York YO10 5YW, England.
Danielsen
Steffen
S
Schagerlöf
Ulrika
U
Turkenburg
Johan P
JP
Davies
Gideon J
GJ
Wilson
Keith S
KS
Taylor
Edward J
EJ
D000595:Amino Acid Sequence; D001232:Aspergillus fumigatus / Q000201:enzymology*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009113:Muramidase / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment
D009113:Muramidase
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