ArticleJournal of bacteriology2012
Crystal structure of the catalytic domain of the Bacillus cereus SleB protein, important in cortex peptidoglycan degradation during spore germination.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 46 citations in OpenAlex.
- YpeB stability affects germination possibly through delaying SleB activity inJournal of bacteriology · 2026Article
- Structural Characterization of Lytic Transglycosylase SltB2 ofACS omega · 2025Article
- Structural and functional analysis ofMicrobiology (Reading, England) · 2025Article
- Physicochemical, genomic, and phenotypic characterization ofMicrobiology spectrum · 2025Article
- Structure of MltG from Mycobacterium abscessus reveals structural plasticity between composed domains.IUCrJ · 2024Article
- Genomic analysis of Salmonella bacteriophages revealed multiple endolysin ORFs and importance of ligand-binding site of receptor-binding protein.FEMS microbiology ecology · 2024Article
- Identification of type VI secretion system effector-immunity pairs using structural bioinformatics.Molecular systems biology · 2024Article
- Loss of the Rhodobacter capsulatus Serine Acetyl Transferase Gene,Applied and environmental microbiology · 2022Article
- A Novel Phage Indirectly Regulates Diatom Growth by Infecting a Diatom-Associated Biofilm-Forming Bacterium.Applied and environmental microbiology · 2022Article
- Horizontally acquired antibacterial genes associated with adaptive radiation of ladybird beetles.BMC biology · 2021Article
- Suboptimal Bacillus licheniformis and Bacillus weihenstephanensis Spore Incubation Conditions Increase Heterogeneity of Spore Outgrowth Time.Applied and environmental microbiology · 2020Article
- Structural and functional analyses of the N-terminal domain of the A subunit of aProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Cell Wall Hydrolases in Bacteria: Insight on the Diversity of Cell Wall Amidases, Glycosidases and Peptidases Toward Peptidoglycan.Frontiers in microbiology · 2019Review
- Lytic transglycosylases: concinnity in concision of the bacterial cell wall.Critical reviews in biochemistry and molecular biology · 2017Review
- Crystal Structures of the SpoIID Lytic Transglycosylases Essential for Bacterial Sporulation.The Journal of biological chemistry · 2016Article
- Identification of MltG as a potential terminase for peptidoglycan polymerization in bacteria.Molecular microbiology · 2016Article
- Role of YpeB in cortex hydrolysis during germination of Bacillus anthracis spores.Journal of bacteriology · 2014Article
- Function of the SpoVAEa and SpoVAF proteins of Bacillus subtilis spores.Journal of bacteriology · 2014Article
- Germination of spores of Bacillus species: what we know and do not know.Journal of bacteriology · 2014Review
- Spore germination mediated by Bacillus megaterium QM B1551 SleL and YpeB.Journal of bacteriology · 2014Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The SleB protein is one of two redundant cortex-lytic enzymes (CLEs) that initiate the degradation of cortex peptidoglycan (PG), a process essential for germination of spores of Bacillus species, including Bacillus anthracis. SleB has been characterized as a soluble lytic transglycosylase that specifically recognizes spore cortex PG and catalyzes the cleavage of glycosidic bonds between N-acetylmuramic acid (NAM) and N-acetylglucosamine residues with concomitant formation of a 1,6-anhydro bond in the NAM residue. We found that like the full-length Bacillus cereus SleB, the catalytic C-terminal domain (SleB(C)) exhibited high degradative activity on cortex PG in vitro, although SleB's N-terminal domain, thought to bind PG, was inactive. The 1.85-Å crystal structure of SleB(C) reveals an ellipsoid molecule with two distinct domains dominated by either α helices or β strands. The overall fold of SleB closely resembles that of the catalytic domain of the family 1 lytic transglycosylases but with a completely different topological arrangement. Structural analysis shows that an invariant Glu157 of SleB is in a position equivalent to that of the catalytic glutamate in other lytic transglycosylases. Indeed, SleB bearing a Glu157-to-Gln mutation lost its cortex degradative activity completely. In addition, the other redundant CLE (called CwlJ) in Bacillus species likely has a three-dimensional structure similar to that of SleB, including the invariant putative catalytic Glu residue. SleB and CwlJ may offer novel targets for the development of anti-spore agents.
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