Structural highlights
Function
D5DRI0_PRIM1
Publication Abstract from PubMed
The crystal structure of the C-terminal domain of the Bacillus megaterium YpeB protein has been solved by X-ray crystallography to 1.80 A 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. This article is protected by copyright. All rights reserved.
Crystal structure of the PepSY-containing domain of the YpeB protein involved in germination of Bacillus spores.,Ustok FI, Chirgadze DY, Christie G Proteins. 2015 Jul 28. doi: 10.1002/prot.24868. PMID:26219275[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ustok FI, Chirgadze DY, Christie G. Crystal structure of the PepSY-containing domain of the YpeB protein involved in germination of Bacillus spores. Proteins. 2015 Jul 28. doi: 10.1002/prot.24868. PMID:26219275 doi:http://dx.doi.org/10.1002/prot.24868
