CASEINOLYTIC PROTEASES

大肠杆菌Ile酪蛋白水解酶由两个组分组成 蛋白酶亚基CIPP和ATPase亚基CIPA。完全活动的CIPP 已在大肠杆菌中过度表达，并纯化至均一。质量 STEM的测量结果表明，它是一个十四聚体。在……里面 污渍，它看起来像两个堆叠的七元环。小角度 测定了ClpP的X-射线和中子散射曲线。 解决方案。根据这些数据建立了一个圆柱体的模型。 轴向气孔。孔的大小与在 伴侣蛋白。CIPP已经结晶，上述数据。 已经被用来帮助解决X射线结构。几种半胱氨酸 对突变体进行了工程设计和Au标记，并在茎中进行了检查以帮助 在结构的确定中。CIPA已在 茎。初步样品不是很好，但更好的尝试 随着更好的提纯样本正在进行中。CIPA组件可以是 六角体。最终目标是查看CIPP和 CIPA。

Ile caseinolytic protease from E. coli is comprised of two subunits ihe protease, CIpP, and the ATPase, CIpA. Fully active CIpP has been over-expressed in R coli and purified to homogeneity. Mass measurements from the STEM indicate that it is a tetradecamer. In stain, it appears as two stacked seven-member rings. Small angle X-ray and neutron scattering curves were determined for ClpP in solution. A model was derived from these data of a cylinder with an axial pore. Ile size of the pore is similar to that found in chaperone proteins. CIpP has been crystallized and the above data. has been used to help solve the x-ray structure. Several cysteine mutants were engineered and Au-labeled and examined in the STEK to aid in the determination of the structure. CIpA has been examined in the STEM. Preliminary samples were not very good but finther attempts with better purified samples are underway. The CIpA component may be hexameric. The final goal is to look at the interaction of CIpP and CIpA.