Crystallization and preliminary X-ray diffraction analysis of a novel β-L-arabinofuranosidase (HypBA1) from Bifidobacterium longum

被引：3
|
作者：
Zhu, Zhen [1 ]
He, Miao [1 ]
Huang, Chun-Hsiang [2 ]
Ko, Tzu-Ping [3 ]
Zeng, Yi-Fang [4 ]
Huang, Yu-Ning [4 ]
Jia, Shiru [1 ]
Lu, Fuping [1 ]
Liu, Je-Ruei [4 ,5 ]
Guo, Rey-Ting [2 ]
机构：
[1] Tianjin Univ Sci & Technol, Coll Biotechnol, Tianjin Key Lab Ind Microbiol, Tianjin 300457, Peoples R China
[2] Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Ind Enzymes Natl Engn Lab, Tianjin 300308, Peoples R China
[3] Acad Sinica, Inst Biol Chem, Taipei 115, Taiwan
[4] Natl Taiwan Univ, Inst Biotechnol, Taipei 106, Taiwan
[5] Natl Taiwan Univ, Dept Anim Sci & Technol, Taipei 106, Taiwan
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2014年 / 70卷
基金：
中国国家自然科学基金;
关键词：
EXTENSIN;
D O I：
10.1107/S2053230X14001812
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
The beta-L-arabinofuranosidase (HypBA1) from Bifidobacterium longum JCM 1217 hydrolyzes the beta-1,2-linked arabinofuranose disaccharide to release L-arabinoses. HypBA1 was classified into glycoside hydrolase family 127 (GH127) by the CAZy website (http://www.cazy.org/). The enzyme was expressed in Escherichia coli and the purified recombinant protein was crystallized. Crystals belonging to the primitive hexagonal space group P3(x)21, with unit-cell parameters a = b = 75.9, c = 254.0 angstrom, were obtained by the sitting-drop vapour-diffusion method and diffracted to 2.78 angstrom resolution. A BLASTP search (http://blast.ncbi.nlm.nih.gov/) of the Protein Data Bank did not reveal any similar crystal structures. Structural determination by using SeMet MAD and MIR methods is in progress.
引用
收藏
页码：636 / 638
页数：3
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