4FET

Catalytic domain of germination-specific lytic tansglycosylase SleB from Bacillus anthracis

Summary for 4FET

• Entry DOI: 10.2210/pdb4fet/pdb
• Descriptor: Spore cortex-lytic enzyme prepeptide, SODIUM ION (3 entities in total)
• Functional Keywords: transglycosylase, cortex hydrolase domain, sodium ion, semet, cortex, hydrolase
• Biological source: Bacillus anthracis (anthrax,anthrax bacterium)
• Total number of polymer chains: 2
• Total formula weight: 48787.80

Authors

Jing, X.,Heffron, J.,Popham, D.L.,Schubot, F.D. (deposition date: 2012-05-30, release date: 2012-07-25, Last modification date: 2024-10-30)

Primary citation

Jing, X.,Robinson, H.R.,Heffron, J.D.,Popham, D.L.,Schubot, F.D.
The catalytic domain of the germination-specific lytic transglycosylase SleB from Bacillus anthracis displays a unique active site topology.
Proteins, 80:2469-2475, 2012

PubMed 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.

PubMed: 22777830
DOI: 10.1002/prot.24140

Experimental method

X-RAY DIFFRACTION (1.909 Å)