Open AccessPreliminary crystallographic studies of purine nucleoside phosphorylase from the cariogenic pathogen Streptococcus mutans
Author(s) -
Hou QiaoMing,
Liu Xiang,
Brostromer Erik,
Li LanFen,
Su XiaoDong
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109045059
Subject(s) - purine nucleoside phosphorylase , streptococcus mutans , purine , pathogen , chemistry , microbiology and biotechnology , biochemistry , biology , bacteria , enzyme , genetics
The punA 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 α‐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 Å resolution at best. The crystals belonged to space group H 3, with unit‐cell parameters a = b = 113.0, c = 60.1 Å.