[Molecular docking of Bacillus pumilus xylanase and xylan substrate using computer modeling].
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.
Lin
Jin-Xia
JX
Key Laboratory of Industrial Biotechnology, Hua Qiao University, Fujian Quanzhou.
Zhang
Liao-Yuan
LY
Zhang
Guang-Ya
GY
Fang
Bai-Shan
BS
D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology* / Q000235:genetics; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D001483:Base Sequence; D003198:Computer Simulation; D043364:Endo-1,4-beta Xylanases / Q000235:genetics / Q000378:metabolism*; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D013379:Substrate Specificity; D014990:Xylans / Q000235:genetics / Q000378:metabolism