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Structure and function analysis of protein HD73_0859 produced by Bacillus thuringiensis

Issue title: Frontiers in Biomedical Engineering and Biotechnology – Proceedings of the 3rd International Conference on Biomedical Engineering and Biotechnology, 25–28 September 2014, Beijing, China

Article type: Research Article

Authors: Wang, Dandan | Zhang, Nan | Guo, Shuyuan;

Affiliations: School of Life Science, Beijing Institute of Technology, Beijing 100081, China

Note: [] Corresponding author: Shuyuan Guo, School of Life Science, Beijing Institute of Technology, Beijing 100081, China. Tel.: 68914495-803; Fax: (010)-68915956; E-mail: [email protected].

Keywords: Bacillus thuringiensis, HD73_0859, structure, function, analysis

DOI: 10.3233/BME-141220

Journal: Bio-Medical Materials and Engineering, vol. 24, no. 6, pp. 3891-3896, 2014

Published: 2014
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Abstract

HD73_0859 is a secretory protein from Bacillus thuringiensis (Bt). In this study, its structural feature was analyzed and its function was predicted. The results revealed that HD73_0859 is a peptidase consists of a signal peptide, three well-separated SH3_3 domains and one Peptidase_M23 domain. The peptidase belongs to the M23/37-metallopeptidase family, and might have enzymatic activity to cell wall peptidoglycan and some elastins. This paper improves the understanding of both the protein HD73_0859 and the M23/37-metallopeptidases family, and lays a foundation for further experimental testing and theoretical study.

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