The crystal structure of a family GH25 lysozyme from Bacillus anthracis implies a neighboring-group catalytic mechanism with retention of anomeric configuration.
Lysozymes are found in many of the sequence-based families of glycoside hydrolases (www.cazy.org) where they show considerable structural and mechanistic diversity. Lysozymes from glycoside hydrolase family GH25 adopt a (alpha/beta)(5)(beta)(3)-barrel-like fold with a proposal in the literature that these enzymes act with inversion of anomeric configuration; the lack of a suitable substrate, however, means that no group has successfully demonstrated the configuration of the product. Here we report the 3-D structure of the GH25 enzyme from Bacillus anthracis at 1.4A resolution. We show that the active center is extremely similar to those from glycoside hydrolase families GH18, GH20, GH56, GH84, and GH85 implying that, in the absence of evidence to the contrary, GH25 enzymes also act with net retention of anomeric configuration using the neighboring-group catalytic mechanism that is common to this 'super-family' of enzymes.
Martinez-Fleites
Carlos
C
Structural Biology Laboratory, Department of Chemistry, The University of York, YO10 5YW, United Kingdom.
Korczynska
Justyna E
JE
Davies
Gideon J
GJ
Cope
Matthew J
MJ
Turkenburg
Johan P
JP
Taylor
Edward J
EJ
D001408:Bacillus anthracis / Q000201:enzymology*; D055162:Biocatalysis; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D006027:Glycosides / Q000378:metabolism; D006868:Hydrolysis; D008958:Models, Molecular; D009113:Muramidase / Q000737:chemistry* / Q000378:metabolism*
D006027:Glycosides; D009113:Muramidase