Crystallization and preliminary crystallographic analysis of two Streptococcus agalactiae proteins: the family II inorganic pyrophosphatase and the serine/threonine phosphatase.

Crystallization and preliminary crystallographic analysis of two Streptococcus agalactiae proteins: the family II inorganic pyrophosphatase and the serine/threonine phosphatase.
复制标题

两种无乳链球菌蛋白的结晶和初步晶体学分析:II族无机焦磷酸酶和丝氨酸/苏氨酸磷酸酶。

DOI:
10.1107/s174430910602954x
复制
发表时间:
2006
期刊:
Acta crystallographica. Section F, Structural biology and crystallization communications
影响因子:
--
通讯作者:
Goldman,Adrian
Goldman,Adrian
中科院分区:
--
文献类型:
--
作者:
Rantanen,MikaK;Lehtiö,Lari;Rajagopal,Lakshmi;Rubens,CraigE;Goldman,Adrian

文献摘要

相似文献

感染人类新生儿并引起败血症和脑膜炎的无乳链球菌最近被证明具有真核生物样丝氨酸/苏氨酸蛋白磷酸化信号级联。通过它们的靶蛋白,S.无乳链球菌Ser/Thr激酶和Ser/Thr磷酸酶共同控制该生物体的生长以及形态和毒力。目标之一是S。无乳家族II无机焦磷酸酶。因此,无机焦磷酸酶和丝氨酸/苏氨酸磷酸酶已被纯化和结晶,并从它们的晶体中收集衍射数据。使用XDS处理数据。无机焦磷酸酶晶体衍射至2.80 nm,Ser/Thr磷酸酶晶体衍射至2.65 nm。  初步的结构溶液实验表明,结构溶液将在这两种情况下是成功的。解决参与这一级联反应的蛋白质结构是从原子细节上理解这一现象的第一步。
Streptococcus agalactiae, which infects human neonates and causes sepsis and meningitis, has recently been shown to possess a eukaryotic-like serine/threonine protein phosphorylation signalling cascade. Through their target proteins, the S. agalactiae Ser/Thr kinase and Ser/Thr phosphatase together control the growth as well as the morphology and virulence of this organism. One of the targets is the S. agalactiae family II inorganic pyrophosphatase. The inorganic pyrophosphatase and the serine/threonine phosphatase have therefore been purified and crystallized and diffraction data have been collected from their crystals. The data were processed using XDS. The inorganic pyrosphosphatase crystals diffracted to 2.80 Å and the Ser/Thr phosphatase crystals to 2.65 Å. Initial structure-solution experiments indicate that structure solution will be successful in both cases. Solving the structure of the proteins involved in this cascade is the first step towards understanding this phenomenon in atomic detail.