金黄色葡萄球菌 FtsA 的晶体结构。
Crystal structure of FtsA from Staphylococcus aureus.
机构信息
Department of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan.
National Institute of Biomedical Innovation, 7-6-8, Saito-Asagi, Ibaraki, Osaka 567-0085, Japan.
出版信息
FEBS Lett. 2014 May 21;588(10):1879-85. doi: 10.1016/j.febslet.2014.04.008. Epub 2014 Apr 18.
The bacterial cell-division protein FtsA anchors FtsZ to the cytoplasmic membrane. But how FtsA and FtsZ interact during membrane division remains obscure. We have solved 2.2 Å resolution crystal structure for FtsA from Staphylococcus aureus. In the crystals, SaFtsA molecules within the dimer units are twisted, in contrast to the straight filament of FtsA from Thermotoga maritima, and the half of S12-S13 hairpin regions are disordered. We confirmed that SaFtsZ and SaFtsA associate in vitro, and found that SaFtsZ GTPase activity is enhanced by interaction with SaFtsA.
细菌细胞分裂蛋白 FtsA 将 FtsZ 锚定在细胞质膜上。但是 FtsA 和 FtsZ 在膜分裂过程中如何相互作用仍然不清楚。我们已经解决了来自金黄色葡萄球菌的 FtsA 的 2.2 Å 分辨率晶体结构。在晶体中，二聚体单元中的 SaFtsA 分子是扭曲的，与来自海洋栖热菌的直丝 FtsA 形成对比，并且 S12-S13 发夹区域的一半是无序的。我们证实 SaFtsZ 和 SaFtsA 在体外结合，并发现 SaFtsZ GTP 酶活性通过与 SaFtsA 的相互作用而增强。
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