1H, 13C and 15N chemical shift assignments for an intracellular proteinase inhibitor of Bacillus subtilis |
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| Authors: | Qingxin Li Angela Shuyi Chen Shovanlal Gayen CongBao Kang |
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| Institution: | 1. Institute of Chemical and Engineering Sciences, Agency for Science, Technology and Research, Singapore, Singapore
2. Experimental Therapeutics Centre, Agency for Science, Technology and Research, 31 Biopolis Way Nanos, #03-01, 138669, Singapore, Singapore
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| Abstract: | Intracellular proteinases (ISPs) are the main component of the bacilli degradome and a distinctive class in different bacilli. An intracellular proteinase inhibitor of the bacteria Bacillus subtillis was shown to regulate the activity of ISP-1. To study the structure of this inhibitor, we report the resonance assignment for this protein with 119 amino acid. The data will allow us to perform structural study on this inhibitor to understand its mechanism for ISP-1 inhibition. |
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