Purification, crystallization and preliminary crystallographic analysis of the marine -amylase AmyP

被引：4
|
作者：
Yu, Jigang [1 ]
Wang, Chengliang [2 ]
Hu, Yanjin [2 ]
Dong, Yuanqiu [1 ]
Wang, Ying [1 ]
Tu, Xiaoming [2 ]
Peng, Hui [1 ]
Zhang, Xuecheng [1 ]
机构：
[1] Anhui Univ, Sch Life Sci, Hefei 230039, Anhui, Peoples R China
[2] Univ Sci & Technol China, Hefei Natl Lab Phys Sci Microscale, Sch Life Sci, Hefei 230026, Anhui, Peoples R China
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2013年 / 69卷
关键词：
AmyP; -amylase; DEGRADING ALPHA-AMYLASE; STARCH;
D O I：
10.1107/S1744309113001693
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
AmyP is a raw-starch-degrading -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 -cyclodextrin. X-ray diffraction data were collected to a resolution of 2.1 angstrom. The crystal belonged to space group P21212, with unit-cell parameters a = 129.824, b = 215.534, c = 79.699 angstrom, = = = 90 degrees, and was estimated to contain two molecules in one asymmetric unit.
引用
收藏
页码：263 / 266
页数：4
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