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The catalytic domain of the germination-specific lytic transglycosylase SleB from Bacillus anthracis displays a unique active site topology
Authors:Xing Jing  Howard R Robinson  Jared D Heffron  David L Popham  Florian D Schubot
Affiliation:Virginia Tech, Department of Biological Sciences, Life Sciences, Blacksburg, Virginia 24061.
Abstract:Bacillus anthracis produces metabolically inactive spores. Germination of these spores requires germination‐specific lytic enzymes (GSLEs) that degrade the unique cortex peptidoglycan to permit resumption of metabolic activity and outgrowth. We report the first crystal structure of the catalytic domain of a GSLE, SleB. The structure revealed a transglycosylase fold with unique active site topology and permitted identification of the catalytic glutamate residue. Moreover, the structure provided insights into the molecular basis for the specificity of the enzyme for muramic‐δ‐lactam‐containing cortex peptidoglycan. The protein also contains a metal‐binding site that is positioned directly at the entrance of the substrate‐binding cleft. Proteins 2012;. © 2012 Wiley Periodicals, Inc.
Keywords:SleB  CwlJ  Bacillus anthracis  spore  germination  lytic transglycosylase  muramic‐δ‐lactam  peptidoglycan  cortex peptidoglycan
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