Structure of a 6-pyruvoyltetrahydropterin synthase homolog from Streptomyces coelicolor

被引:1
|
作者
Spoonamore, James E. [1 ,2 ]
Roberts, Sue A. [1 ,2 ]
Heroux, Annie [3 ]
Bandarian, Vahe [1 ,2 ,4 ]
机构
[1] Univ Arizona, Dept Biochem, Tucson, AZ 85721 USA
[2] Univ Arizona, Dept Mol Biophys, Tucson, AZ 85721 USA
[3] Brookhaven Natl Lab, Dept Biol, Upton, NY 11973 USA
[4] Univ Arizona, Dept Chem, Tucson, AZ 85721 USA
基金
美国国家卫生研究院;
关键词
D O I
10.1107/S1744309108027048
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The X-ray crystal structure of the 6-pyruvoyltetrahydropterin synthase (PTPS) homolog from Streptomyces coelicolor, SCO 6650, was solved at 1.5 angstrom resolution. SCO 6650 forms a hexameric T-fold that closely resembles other PTPS proteins. The biological activity of SCO 6650 is unknown, but it lacks both a required active-site zinc metal ion and the essential catalytic triad and does not catalyze the PTPS reaction. However, SCO 6650 maintains active-site residues consistent with binding a pterin-like substrate.
引用
收藏
页码:875 / 879
页数:5
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