来自天蓝色链霉菌的6-丙酮酰四氢蝶呤合酶同源物的结构
Structure of a 6-pyruvoyltetrahydropterin synthase homolog from Streptomyces coelicolor.
作者信息
Spoonamore James E, Roberts Sue A, Heroux Annie, Bandarian Vahe
机构信息
Department of Biochemistry, University of Arizona, Tucson, AZ 85721, USA.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Oct 1;64(Pt 10):875-9. doi: 10.1107/S1744309108027048. Epub 2008 Sep 30.
Abstract
The X-ray crystal structure of the 6-pyruvoyltetrahydropterin synthase (PTPS) homolog from Streptomyces coelicolor, SCO 6650, was solved at 1.5 A 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.
摘要
天蓝色链霉菌（Streptomyces coelicolor）的6-丙酮酰四氢蝶呤合酶（PTPS）同源物SCO 6650的X射线晶体结构在1.5埃分辨率下得到解析。SCO 6650形成一种六聚体T型折叠结构，与其他PTPS蛋白非常相似。SCO 6650的生物学活性未知，但它既缺乏必需的活性位点锌金属离子和关键催化三联体，也不催化PTPS反应。然而，SCO 6650的活性位点残基与结合类蝶呤底物一致。
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