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Crystal structure of the PepSY-containing domain of the YpeB protein involved in germination of bacillus spores

DOI: 10.1002/prot.24868 DOI Help
PMID: 26219275 PMID Help

Authors: Fatma Isik Ustok (University of Cambridge) , Dima Chirgadze (University of Cambridge) , Graham Christie (University of Cambridge)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Proteins: Structure, Function, and Bioinformatics , VOL 83 (10) , PAGES 1914 - 1921

State: Published (Approved)
Published: October 2015
Diamond Proposal Number(s): 9537

Open Access Open Access

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.

Journal Keywords: Cortex Peptidoglycan; Cortex Lytic Enzyme; Sleb; Cwlj; Slel; Inhibitory Protein

Subject Areas: Biology and Bio-materials

Instruments: I04-Macromolecular Crystallography

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