title: Crystal structure of the PepSY-containing domain of the YpeB protein involved in germination of bacillus spores.
abstract: The crystal structure of the C-terminal domain of the Bacillus megaterium YpeB protein has been solved by X-ray crystallography to 1.80-Å resolution. The full-length protein is essential in stabilising the SleB cortex lytic enzyme in Bacillus spores, and may have a role in regulating SleB activity during spore germination. The YpeB-C crystal structure comprises three tandemly repeated PepSY domains, which are aligned to form an extended laterally compressed molecule. A predominantly positively charged region located in the second PepSY domain may provide a site for protein interactions that are important in stabilising SleB and YpeB within the spore.
authors.affiliation: Department of Chemical Engineering and Biotechnology, Institute of Biotechnology, University of Cambridge, Cambridge, United Kingdom.
authors.forename: Fatma Işık
authors.initials: FI
authors.lastname: Üstok
authors.affiliation: Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom.
authors.forename: Dimitri Y
authors.initials: DY
authors.lastname: Chirgadze
authors.affiliation: Department of Chemical Engineering and Biotechnology, Institute of Biotechnology, University of Cambridge, Cambridge, United Kingdom.
authors.forename: Graham
authors.initials: G
authors.lastname: Christie
mesh_terms: D000595:Amino Acid Sequence; D001410:Bacillus megaterium / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D013171:Spores, Bacterial / Q000201:enzymology*
chemical_list: D001426:Bacterial Proteins
keywords: CwlJ; SleB; SleL; cortex lytic enzyme; cortex peptidoglycan; inhibitory protein