Molecular docking of Bacillus pumilus xylanase and xylan substrate using computer modeling.
- Author:
Jin-Xia LIN
1
;
Liao-Yuan ZHANG
;
Guang-Ya ZHANG
;
Bai-Shan FANG
Author Information
1. Key Laboratory of Industrial Biotechnology, Hua Qiao University, Fujian Quanzhou.
- Publication Type:Journal Article
- MeSH:
Amino Acid Sequence;
Bacillus;
enzymology;
genetics;
Bacterial Proteins;
genetics;
metabolism;
Base Sequence;
Computer Simulation;
Endo-1,4-beta Xylanases;
genetics;
metabolism;
Models, Chemical;
Models, Molecular;
Molecular Sequence Data;
Protein Binding;
Substrate Specificity;
Xylans;
genetics;
metabolism
- From:
Chinese Journal of Biotechnology
2007;23(4):715-718
- CountryChina
- Language:Chinese
-
Abstract:
Bacillus pumilus xylanase was cloned and sequenced. Based on the tertiary structure that originated from homology modeling, the potential active pocket was searched and ligand-protein docking was performed using relative softwares. The information extracted from the molecular docking is analyzed; several amino acid residues might play a vital role in the xylanase catalytic reaction are obtained to instruct the further modification of xylanase directed-evolution.
