4fet

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

spinqualitylabelsall models 4fet, resolution 1.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4fet is a 2 chain structure with sequence from Bacillus anthracis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.909Å Ligands: MSE, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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