Majce Vita, Ruane Karen M, Gobec Stanislav, Roper David I
School of Life Sciences, University of Warwick, Gibbet Hill Road, Coventry, West Midlands CV4 7AL, England.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 May 1;69(Pt 5):503-5. doi: 10.1107/S1744309113005344. Epub 2013 Apr 30.
The ATP-dependent UDP-MurNAc-tripeptide:D-Ala-D-Ala ligase MurF catalyses the last step in the cytoplasmic phase of peptidoglycan biosynthesis, which is critical in the formation of the bacterial cell wall and in the recycling of peptidoglycan intermediates. In this study, the crystallization of MurF from the Gram-negative pathogen Pseudomonas aeruginosa in the presence of its UDP-MurNAc-tripeptide substrate is reported. The crystals belonged to space group P212121, with unit-cell parameters a = 57.81, b = 87.29, c = 92.61 Å, and data were collected to 1.92 Å resolution, allowing study of the enzyme in the substrate-liganded form for the first time.
ATP 依赖性 UDP-N-乙酰胞壁酸-三肽:D-丙氨酰-D-丙氨酸连接酶 MurF 催化肽聚糖生物合成细胞质阶段的最后一步,这在细菌细胞壁的形成以及肽聚糖中间体的循环利用中至关重要。在本研究中,报道了来自革兰氏阴性病原体铜绿假单胞菌的 MurF 在其 UDP-N-乙酰胞壁酸-三肽底物存在下的结晶情况。晶体属于空间群 P212121,晶胞参数 a = 57.81、b = 87.29、c = 92.61 Å,数据收集至 1.92 Å 分辨率,首次使得对处于底物结合形式的该酶进行研究成为可能。