Crystallization and preliminary crystallographic analysis of the soluble alpha-glycerophosphate oxidase from Streptococcus sp.
Crystallization and preliminary crystallographic analysis of the soluble alpha-glycerophosphate oxidase from Streptococcus sp.
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链球菌可溶性 α-甘油磷酸氧化酶的结晶和初步晶体学分析。
DOI：
10.1107/s0907444901018169
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发表时间：
2002
期刊：
影响因子：
--
通讯作者：
Karplus,PAndrew
中科院分区：
文献类型：
--
作者：
Finnerty,CaseyM;Charrier,Véronique;Claiborne,Al;Karplus,PAndrew
来自链球菌的可溶性 FAD 依赖性 α-甘油磷酸氧化酶 (GlpO) 单晶。使用微播种和悬滴蒸汽平衡方法获得。使用同步加速器 X 射线辐射从这些晶体中收集分辨率为 2.4 Å 的衍射数据。 GlpO 与几种细菌和线粒体 α-甘油磷酸脱氢酶具有 >30% 的同一性，尽管 GlpO 包含 50-52 个残基的独特插入片段，这似乎对于有效还原黄素很重要。目前的工作是确定 GlpO 结构的重要第一步，这将为了解这种有趣的黄素酶及其同系物的功能提供见解。
Single crystals of soluble FAD-dependent α-glycerophosphate oxidase (GlpO) from Streptococcus sp. were obtained using the microseeding and hanging-drop vapor-equilibrium methods. Synchrotron X-ray radiation was used to collect diffraction data to 2.4 Å resolution from these crystals. GlpO shares >30% identity with several bacterial and mitochondrial α-glycerophosphate dehydrogenases, although the GlpOs contain a 50–52-residue unique insert that appears to be important for efficient flavin reduction. The present work is an important first step in determining the structure of GlpO, which should provide insights on the function of this interesting flavoenzyme and its homologs.