Crystal structure of the PepSY‐containing domain of the YpeB protein involved in germination of bacillus spores |
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Authors: | Fatma I??k Üstok Dimitri Y Chirgadze Graham Christie |
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Institution: | 1. Department of Chemical Engineering and Biotechnology, Institute of Biotechnology, University of Cambridge, Cambridge, United Kingdom;2. Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom |
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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. Proteins 2015; 83:1914–1921. © 2015 Wiley Periodicals, Inc. |
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Keywords: | cortex peptidoglycan cortex lytic enzyme SleB CwlJ SleL inhibitory protein |
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