Crystal structure of the PepSY-containing domain of the YpeB protein involved in germination of bacillus spores.
Type
Article
Change log
Authors
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.
Description
Keywords
CwlJ, SleB, SleL, cortex lytic enzyme, cortex peptidoglycan, inhibitory protein, Amino Acid Sequence, Bacillus megaterium, Bacterial Proteins, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Protein Structure, Tertiary, Spores, Bacterial
Journal Title
Proteins
Conference Name
Journal ISSN
0887-3585
1097-0134
1097-0134
Volume Title
83
Publisher
Wiley
Publisher DOI
Sponsorship
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.