Kaushik Sanket, Singh Avinash, Sinha Mau, Kaur Punit, Sharma Sujata, Singh Tej P
Department of Biophysics, All India Institute of Medical Sciences, New Delhi 110 029, India.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jun;69(Pt 6):653-6. doi: 10.1107/S1744309113011214. Epub 2013 May 24.
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 Å, and contained four molecules in the asymmetric unit. The complete structure determination of AbDHDPR is in progress.
鲍曼不动杆菌是一种毒性很强的病原菌，对目前大多数可用抗生素具有抗性。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。二氢吡啶二羧酸还原酶（DHDPR）是一种重要的酶，参与细菌中导致L-赖氨酸产生的生物合成途径。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。晶体采用悬滴气相扩散法，以聚乙二醇3350作为沉淀剂生长。晶体属于正交晶系空间群P222，晶胞参数a = 80.0，b = 100.8，c = 147.6 Å，不对称单元中包含四个分子。AbDHDPR的完整结构测定正在进行中。
