Preliminary crystallographic studies of purine nucleoside phosphorylase from the cariogenic pathogen Streptococcus mutans

被引:2
作者
Hou, Qiao-Ming [1 ,2 ]
Liu, Xiang [2 ]
Brostromer, Erik [2 ]
Li, Lan-Fen [2 ]
Su, Xiao-Dong [1 ,2 ]
机构
[1] Peking Univ, Shenzhen Grad Sch, Shenzhen 518055, Peoples R China
[2] Peking Univ, Natl Lab Prot Engn & Plant Genet Engn, Coll Life Sci, Beijing 100871, Peoples R China
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2009年 / 65卷
基金
中国国家自然科学基金;
关键词
CRYSTAL-STRUCTURE; COMPLEX; ANALOG;
D O I
10.1107/S1744309109045059
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The pun Lambda gene of the cariogenic pathogen Streptococcus mutans encodes purine nucleoside phosphorylase (PNP), which is a pivotal enzyme in the nucleotide-salvage pathway, catalyzing the phosphorolysis of purine nucleosides to generate purine bases and alpha-ribose 1-phosphate. In the present work, the PNP protein was expressed in Escherichia coli strain BL21 (DE3) in a soluble form at a high level. After purification of the PNP enzyme, the protein was crystallized using the sitting-drop vapour-diffusion technique; the crystals diffracted to 1.6 angstrom resolution at best. The crystals belonged to space group H3, with unit-cell parameters a = b = 113.0, c = 60.1 angstrom.
引用
收藏
页码:1289 / 1291
页数:3
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