首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Preliminary X-ray diffraction analysis of octaprenyl pyrophosphate synthase from Escherichia coli
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Preliminary X-ray diffraction analysis of octaprenyl pyrophosphate synthase from Escherichia coli

机译:大肠杆菌八邻戊二烯基焦磷酸合酶的X射线初步分析

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摘要

Octaprenyl pyrophosphate synthase (OPPs), which belongs to the E-type prenyltransferase family, catalyses the successive condensation of farnesyl pyrophosphate with five isopentenyl pyrophosphate molecules to form trans-C40-octaprenyl pyrophosphate (OPP). OPP is essential for the biosynthesis of bacterial ubiquinone or menaquinone side chains, which play an important role in the electron-transport system. Here, Escherichia coli OPPs was expressed, purified and crystallized. The crystals, which belonged to the orthorhombic space group P21212, with unit-cell parameters a = 117.0, b = 128.4, c = 46.4 angstrom, were obtained by the sitting-drop vapour-diffusion method and diffracted to 2.2 angstrom resolution. Initial phase determination by molecular replacement (MR) clearly indicated that the crystal contained one homodimer per asymmetric unit. Further model building and structural refinement are in progress.
机译:属于E型异戊烯基转移酶家族的八碳烯基焦磷酸合酶(OPP)催化法呢基焦磷酸与五个异戊烯基焦磷酸分子的连续缩合,从而形成反式C40-八烯基焦磷酸(OPP)。 OPP对于细菌泛醌或甲萘醌侧链的生物合成至关重要,它们在电子传输系统中起着重要作用。在此,表达,纯化和结晶大肠杆菌OPP。通过坐滴蒸气扩散法获得晶体,该晶体属于正交晶体空间群P21212,其晶胞参数为a = 117.0,b = 128.4,c = 46.4埃,并衍射至2.2埃分辨率。通过分子置换(MR)进行的初始相确定清楚地表明,该晶体每个不对称单元包含一个均二聚体。进一步的模型构建和结构改进正在进行中。

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