2WAG

The Structure of a family 25 Glycosyl hydrolase from Bacillus anthracis.

Summary for 2WAG

• Entry DOI: 10.2210/pdb2wag/pdb
• Descriptor: LYSOZYME, PUTATIVE, POLYETHYLENE GLYCOL (N=34), SULFATE ION, ... (6 entities in total)
• Functional Keywords: hydrolase, gh25, lysin, lysozyme, bacillus anthracis
• Biological source: BACILLUS ANTHRACIS
• Total number of polymer chains: 1
• Total formula weight: 34418.28

Authors

Martinez-Fleites, C.,Korczynska, J.E.,Cope, M.,Turkenburg, J.P.,Taylor, E.J. (deposition date: 2009-02-06, release date: 2009-06-23, Last modification date: 2023-12-13)

Primary citation

Martinez-Fleites, C.,Korczynska, J.E.,Cope, M.,Turkenburg, J.P.,Taylor, E.J.
The Crystal Structure of a Family Gh25 Lysozyme from Bacillus Anthracis Implies a Neighboring-Group Catalytic Mechanism with Retention of Anomeric Configuration
Carbohydr.Res., 344:1753-, 2009

PubMed Abstract: 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.

PubMed: 19595298
DOI: 10.1016/J.CARRES.2009.06.001

Experimental method

X-RAY DIFFRACTION (1.4 Å)