Purification, crystallization and preliminary X-ray diffraction studies of N-acetylglucosaminephosphate mutase from Candida albicans

被引：3
|
作者：
Nishitani, Y
Maruyama, D
Nonaka, T
Kita, A
Fukami, TA
Mio, T
Yamada-Okabe, H
Yamada-Okabe, T
Miki, K [1 ]
机构：
[1] Kyoto Univ, Grad Sch Sci, Dept Chem, Sakyo Ku, Kyoto 6068502, Japan
[2] Chugai Pharmaceut Co Ltd, Kamakura Res Lab, Kanagawa 2478530, Japan
[3] Yokohama City Univ, Sch Med, Dept Hyg, Kanazawa Ku, Yokohama, Kanagawa 2360004, Japan
[4] Harima Inst, RIKEN SPring 8 Ctr, Mikazuki, Hyogo 6785148, Japan
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2006年 / 62卷
关键词：
D O I：
10.1107/S1744309106010177
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
N-acetylglucosamine-phosphate mutase (AGM1) is an essential enzyme in the synthesis of UDP-N-acetylglucosamine ( UDP-GlcNAc) in eukaryotes and belongs to the alpha-D-phosphohexomutase superfamily. AGM1 from Candida albicans (CaAGM1) was purified and crystallized by the sitting-drop vapour-diffusion method. The crystals obtained belong to the primitive monoclinic space group P2(1), with unit-cell parameters a = 60.2, b = 130.2, c = 78.0 angstrom, beta = 106.7 degrees. The crystals diffract X-rays to beyond 1.8 angstrom resolution using synchrotron radiation.
引用
收藏
页码：419 / 421
页数：3
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