Structural highlights
Function
A0A6L8PLE1_BACAN
Publication Abstract from PubMed
Bacillus anthracisproduces 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-delta-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. (c) 2012 Wiley Periodicals, Inc.
The catalytic domain of the germination-specific lytic transglycosylasesleb from bacillus anthracisdisplays a unique active site topology.,Jing X, Robinson HR, Heffron J, Popham DL, Schubot FD Proteins. 2012 Jul 7. doi: 10.1002/prot.24140. PMID:22777830[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jing X, Robinson HR, Heffron J, Popham DL, Schubot FD. The catalytic domain of the germination-specific lytic transglycosylasesleb from bacillus anthracisdisplays a unique active site topology. Proteins. 2012 Jul 7. doi: 10.1002/prot.24140. PMID:22777830 doi:10.1002/prot.24140
