Crystallization and preliminary X-ray studies of an electron-transfer complex of ferredoxin and ferredoxin-dependent glutamate synthase from the cyanobacterium Leptolyngbya boryana
Crystallization and preliminary X-ray studies of an electron-transfer complex of ferredoxin and ferredoxin-dependent glutamate synthase from the cyanobacterium Leptolyngbya boryana
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来自蓝藻 Leptolyngbya boryana 的铁氧还蛋白和铁氧还蛋白依赖性谷氨酸合酶的电子转移复合物的结晶和初步 X 射线研究
DOI：
10.1107/s1744309112003387
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发表时间：
2012
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et al
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作者：
Shinmura K.;et al
铁氧还蛋白（Ferredoxin，Fd）依赖的谷氨酸合酶（Ferredoxin dependent glutamate synthase，Fd-GOGAT）是氮同化过程中的关键酶，催化Gln和2-酮戊二酸（2-oxoglutarate）双电子还原转化为Glu。Fd作为Fd-GOGAT的电子供体，两种蛋白质形成瞬时电子转移复合物。在这项研究中，这两种蛋白质共结晶使用悬滴气相扩散法。收集衍射数据并以2.65 nm分辨率进行处理。 晶体属P43空间群，晶胞参数a = B = 84.95，c = 476.31 nm。
Ferredoxin (Fd) dependent glutamate synthase (Fd-GOGAT) is a key enzyme involved in nitrogen assimilation that catalyzes the two-electron reductive conversion of Gln and 2-oxoglutarate to two molecules of Glu. Fd serves as an electron donor for Fd-GOGAT and the two proteins form a transient electron-transfer complex. In this study, these two proteins were cocrystallized using the hanging-drop vapour-diffusion method. Diffraction data were collected and processed at 2.65 Å resolution. The crystals belonged to space group P43, with unit-cell parameters a = b = 84.95, c = 476.31 Å.