Structure and function analysis of protein HD73_0859 produced by Bacillus thuringiensis

Dandan Wang; Nan Zhang; Shuyuan Guo

doi:10.3233/BME-141220

Structure and function analysis of protein HD73_0859 produced by Bacillus thuringiensis

Biomed Mater Eng. 2014;24(6):3891-6. doi: 10.3233/BME-141220.

Authors

Dandan Wang¹, Nan Zhang¹, Shuyuan Guo¹

Affiliation

¹ School of Life Science, Beijing Institute of Technology, Beijing 100081, China.

PMID: 25227107
DOI: 10.3233/BME-141220

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.

Keywords: Bacillus thuringiensis; HD73_0859; analysis; function; structure.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Bacillus thuringiensis / enzymology*
Enzyme Activation
Metalloproteases / chemistry*
Metalloproteases / ultrastructure*
Molecular Sequence Data
Protein Conformation

Substances

Metalloproteases