Structure and function analysis of protein HD73-0859 produced by Bacillus thuringiensis

Wang Dandan; Zhang Nan; Guo Shuyuan

doi:10.3233/BME-141220

Structure and function analysis of protein HD73-0859 produced by Bacillus thuringiensis

Wang Dandan
, Zhang Nan
, Guo Shuyuan^*

^*Corresponding author for this work

School of Life Science

Beijing Institute of Technology

Research output: Contribution to journal › Article › peer-review

2 Citations (Scopus)

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.

Original language	English
Pages (from-to)	3891-3896
Number of pages	6
Journal	Bio-Medical Materials and Engineering
Volume	24
Issue number	6
DOIs	https://doi.org/10.3233/BME-141220
Publication status	Published - 2014

Keywords

Analysis
Bacillus thuringiensis
Function
HD73-0859
Structure

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10.3233/BME-141220

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title = "Structure and function analysis of protein HD73-0859 produced by Bacillus thuringiensis",

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 = "Analysis, Bacillus thuringiensis, Function, HD73-0859, Structure",

author = "Wang Dandan and Zhang Nan and Guo Shuyuan",

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AU - Nan, Zhang

AU - Shuyuan, Guo

PY - 2014

Y1 - 2014

N2 - 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.

AB - 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.

KW - Analysis

KW - Bacillus thuringiensis

KW - Function

KW - HD73-0859

KW - Structure

UR - https://www.scopus.com/pages/publications/84907274633

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DO - 10.3233/BME-141220

M3 - Article

C2 - 25227107

AN - SCOPUS:84907274633

SN - 0959-2989

VL - 24

SP - 3891

EP - 3896

JO - Bio-Medical Materials and Engineering

JF - Bio-Medical Materials and Engineering

IS - 6

ER -

Structure and function analysis of protein HD73-0859 produced by Bacillus thuringiensis

Abstract

Keywords

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