Crystal structure of the PepSY-containing domain of the YpeB protein involved in germination of Bacillus spores
Proteins: Structure, Function, and Bioinformatics
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Üstok, F. I., Chirgadze, D., & Christie, G. (2015). Crystal structure of the PepSY-containing domain of the YpeB protein involved in germination of Bacillus spores. Proteins: Structure, Function, and Bioinformatics, 83 1914-1921. https://doi.org/10.1002/prot.24868
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.
cortex peptidoglycan, cortex lytic enzyme, SleB, CwlJ, SleL, inhibitory protein
The author acknowledges support from various sources including the new lecturers' start up funding from Cambridge University and a donation from the Government Decontamination Service.
External DOI: https://doi.org/10.1002/prot.24868
This record's URL: https://www.repository.cam.ac.uk/handle/1810/249128