鲍曼不动杆菌UDP-N-乙酰胞壁酰三肽-D-丙氨酰-D-丙氨酸连接酶（MurF）的纯化、结晶及初步X射线晶体学分析
Purification, crystallization and preliminary X-ray crystallographic analysis of the UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase (MurF) from Acinetobacter baumannii.
作者信息
An Young Jun, Jeong Chang-Sook, Yu Jeong Hee, Chung Kyung Min, Cha Sun-Shin
机构信息
Marine Biotechnology Research Division, Korea Institute of Ocean Science and Technology, Ansan, Kyonggi-do 426-744, Republic of Korea.
Department of Microbiology and Immunology, Chonbuk National University Medical School, Jeonju, Jeonbuk 561-756, Republic of Korea.
出版信息
Acta Crystallogr F Struct Biol Commun. 2014 Jul;70(Pt 7):976-8. doi: 10.1107/S2053230X14009984. Epub 2014 Jun 19.
The emergence and global spread of multidrug-resistant Acinetobacter baumannii strains are major threats to public health. Inhibition of peptidoglycan biosynthesis is an effective strategy for the development of antibiotics. The ATP-dependent UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase (MurF) that is responsible for the last step of peptidoglycan biosynthesis is a validated target for the development of antibiotics. Crystals of A. baumannii MurF in complex with ATP were grown by the microbatch crystallization method at 295 K. The crystals belonged to space group P322₁, with unit-cell parameters a=b=85.42, c=129.86 Å. Assuming the presence of one molecule in the asymmetric unit, the solvent content was estimated to be about 54.32%.
多重耐药鲍曼不动杆菌菌株的出现和全球传播是对公共卫生的主要威胁。抑制肽聚糖生物合成是开发抗生素的有效策略。负责肽聚糖生物合成最后一步的ATP依赖性UDP-N-乙酰胞壁酰-三肽-D-丙氨酰-D-丙氨酸连接酶（MurF）是开发抗生素的一个经过验证的靶点。通过微量分批结晶法在295 K下培养了与ATP结合的鲍曼不动杆菌MurF晶体。晶体属于空间群P322₁，晶胞参数a=b=85.42，c=129.86 Å。假设不对称单元中存在一个分子，溶剂含量估计约为54.32%。
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