Crystallization and diffraction analysis of β-N-acetylhexosaminidase from Aspergillus oryzae

被引：6
|
作者：
Vanek, Ondrej [2 ,3 ]
Brynda, Jiri [1 ,4 ]
Hofbauerova, Katerina [3 ]
Kukacka, Zdenek [2 ,3 ]
Pachl, Petr [4 ]
Bezouska, Karel [2 ,3 ]
Rezacova, Pavlina [1 ,4 ]
机构：
[1] Acad Sci Czech Republ, Inst Organ Chem & Biochem, CR-16610 Prague, Czech Republic
[2] Charles Univ Prague, Fac Sci, Dept Biochem, Prague 12840, Czech Republic
[3] Acad Sci Czech Republ, Inst Microbiol, CR-14220 Prague, Czech Republic
[4] Acad Sci Czech Republ, Inst Mol Genet, CR-14220 Prague, Czech Republic
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2011年 / 67卷
关键词：
fungal hexosaminidases; glycoproteins; quantitative Edman degradation; CHITIN SYNTHESIS; INTEGRATION;
D O I：
10.1107/S1744309111004945
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Fungal beta-N-acetylhexosaminidases are enzymes that are used in the chemoenzymatic synthesis of biologically interesting oligosaccharides. The enzyme from Aspergillus oryzae was produced and purified from its natural source and crystallized using the hanging-drop vapour-diffusion method. Diffraction data from two crystal forms (primitive monoclinic and primitive tetragonal) were collected to resolutions of 3.2 and 2.4 A, respectively. Electrophoretic and quantitative N-terminal protein-sequencing analyses confirmed that the crystals are formed by a complete biologically active enzyme consisting of a glycosylated catalytic unit and a noncovalently attached propeptide.
引用
收藏
页码：498 / 503
页数：6
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