TY - JOUR
T1 - The crystal structure of a family GH25 lysozyme from Bacillus anthracis implies a neighboring-group catalytic mechanism with retention of anomeric configuration
AU - Martinez-Fleites, Carlos
AU - Korczynska, Justyna E.
AU - Davies, Gideon J.
AU - Cope, Matthew J.
AU - Turkenburg, Johan P.
AU - Taylor, Edward J.
PY - 2009/9/8
Y1 - 2009/9/8
N2 - 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 1.4 angstrom 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. (C) 2009 Elsevier Ltd. All rights reserved.
AB - 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 1.4 angstrom 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. (C) 2009 Elsevier Ltd. All rights reserved.
KW - Lysozyme
KW - Autolysin
KW - Peptidoglycan cleavage
KW - Anthrax
KW - Hexosaminidase
KW - SUBSTRATE-ASSISTED CATALYSIS
KW - PHAGE LYTIC ENZYME
KW - ACTIVE-SITE
KW - MOLECULAR REPLACEMENT
KW - GLYCOSYL HYDROLASES
KW - MUREIN HYDROLASES
KW - CELL-WALL
KW - IDENTIFICATION
KW - RECOGNITION
KW - CHITOBIASE
UR - http://www.scopus.com/inward/record.url?scp=68949170989&partnerID=8YFLogxK
U2 - 10.1016/j.carres.2009.06.001
DO - 10.1016/j.carres.2009.06.001
M3 - Article
SN - 0008-6215
VL - 344
SP - 1753
EP - 1757
JO - CARBOHYDRATE RESEARCH
JF - CARBOHYDRATE RESEARCH
IS - 13
ER -