Son Sang Hyeon, Lee Hyung Ho
Department of Bio and Nano Chemistry, Kookmin University, Seoul 136-702, Republic of Korea.
Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 151-742, Republic of Korea.
Acta Crystallogr F Struct Biol Commun. 2015 Feb;71(Pt 2):194-8. doi: 10.1107/S2053230X15000266. Epub 2015 Jan 28.
Bacterial cytokinesis is accomplished by the Z-ring, which is a polymeric structure that includes the tubulin homologue FtsZ at the division site. ZapD, a Z-ring-associated protein, directly binds to FtsZ and stabilizes the polymerization of FtsZ to form a stable Z-ring during cytokinesis. Structural analysis of ZapD from Escherichia coli was performed to investigate the mechanism of ZapD-mediated FtsZ stabilization and polymerization. ZapD was crystallized using a reservoir solution consisting of 1.5 M lithium sulfate, 0.1 M HEPES pH 7.8, 2%(v/v) polyethylene glycol 400. X-ray diffraction data were collected to 2.95 Å resolution. The crystals belonged to the hexagonal space group P64, with unit-cell parameters a = b = 109.5, c = 106.7 Å, γ = 120.0°. Two monomers were present in the asymmetric unit, resulting in a crystal volume per protein mass (VM) of 3.25 Å(3) Da(-1) and a solvent content of 62.17%.
细菌胞质分裂由Z环完成，Z环是一种聚合物结构，在分裂位点包含微管蛋白同源物FtsZ。ZapD是一种与Z环相关的蛋白，它直接与FtsZ结合，并在胞质分裂期间稳定FtsZ的聚合以形成稳定的Z环。对来自大肠杆菌的ZapD进行结构分析，以研究ZapD介导的FtsZ稳定化和聚合的机制。使用由1.5 M硫酸锂、0.1 M HEPES pH 7.8、2%（v/v）聚乙二醇400组成的储液使ZapD结晶。收集了分辨率为2.95 Å的X射线衍射数据。晶体属于六方空间群P64，晶胞参数a = b = 109.5，c = 106.7 Å，γ = 120.0°。不对称单元中有两个单体，导致每蛋白质质量的晶体体积（VM）为3.25 Å(3) Da(-1)，溶剂含量为62.17%。
