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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Cloning, expression, crystallization and preliminary structural studies of dihydrodipicolinate reductase from Acinetobacter baumannii
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Cloning, expression, crystallization and preliminary structural studies of dihydrodipicolinate reductase from Acinetobacter baumannii

机译：鲍曼不动杆菌双氢吡啶二羧酸还原酶的克隆，表达，结晶及初步结构研究

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摘要

Acinetobacter baumannii is a virulent pathogenic bacterium that is resistant to most currently available antibiotics. Therefore, the design of drugs for the treatment of infections caused by A. baumannii is urgently required. Dihydrodipicolinate reductase (DHDPR) is an important enzyme which is involved in the biosynthetic pathway that leads to the production of l-lysine in bacteria. In order to design potent inhibitors against this enzyme, its detailed three-dimensional structure is required. DHDPR from A. baumannii (AbDHDPR) has been cloned, expressed, purified and crystallized. Here, the preliminary X-ray crystallographic data of AbDHDPR are reported. The crystals were grown using the hanging-drop vapour-diffusion method with PEG 3350 as the precipitating agent The crystals belonged to the orthorhombic space group P222, with unit-cell parameters a = 80.0, b = 100.8, c = 147.6 angstrom, and contained four molecules in the asymmetric unit. The complete structure determination of AbDHDPR is in progress.
机译：鲍曼不动杆菌是对大多数当前可用抗生素具有抗性的致病性致病细菌。因此，迫切需要设计用于治疗由鲍曼不动杆菌引起的感染的药物。二氢吡啶二甲酸酯还原酶（DHDPR）是一种重要的酶，它参与导致细菌产生l-赖氨酸的生物合成途径。为了设计针对该酶的有效抑制剂，需要其详细的三维结构。来自鲍曼不动杆菌的DHDPR（AbDHDPR）已被克隆，表达，纯化和结晶。在此，报道了AbDHDPR的初步X射线晶体学数据。晶体是通过悬滴蒸汽扩散法以PEG 3350作为沉淀剂生长的。晶体属于正交晶空间群P222，晶胞参数a = 80.0，b = 100.8，c = 147.6埃，并包含不对称单元中的四个分子。 AbDHDPR的完整结构确定正在进行中。

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