Purification, crystallization and preliminary crystallographic analysis of the marine α-amylase AmyP
| Autor: | Yanjin Hu, Xiaoming Tu, Chengliang Wang, Jigang Yu, Yuanqiu Dong, Xuecheng Zhang, Hui Peng, Ying Wang |
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| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
Aquatic Organisms
Subfamily Starch Biophysics Beta-Cyclodextrins medicine.disease_cause Crystallography X-Ray Biochemistry chemistry.chemical_compound Structural Biology Genetics medicine Escherichia coli Glycoside hydrolase Amylase biology beta-Cyclodextrins Substrate (chemistry) Condensed Matter Physics Recombinant Proteins Crystallography chemistry Crystallization Communications biology.protein Metagenome alpha-Amylases Alpha-amylase Crystallization |
| Popis: | AmyP is a raw-starch-degrading α-amylase newly identified from a marine metagenome library. It shares low sequence similarity with characterized glycoside hydrolases and was classified into a new subfamily of GH13. In particular, it showed preferential degradation to raw rice starch. Full-length AmyP was cloned and overexpressed in Escherichia coli, then purified and crystallized in the presence of its substrate analogue β-cyclodextrin. X-ray diffraction data were collected to a resolution of 2.1 A. The crystal belonged to space group P21212, with unit-cell parameters a = 129.824, b = 215.534, c = 79.699 A, α = β = γ = 90°, and was estimated to contain two molecules in one asymmetric unit. |
| Databáze: | OpenAIRE |
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