CASEINOLYTIC PROTEASES

来自E.大肠杆菌由两个 蛋白酶亚基ClpP和ATP酶亚基ClpA。 完全激活的CipP 已在大肠杆菌中过表达并纯化至均一。 质量 STEM的测量表明它是十四聚体。 在 染色，它看起来像两个堆叠的七元环。 小角度 X射线和中子散射曲线测定ClpP在 溶液 从这些数据中导出了一个模型， 轴孔 孔的大小类似于 伴侣蛋白 对ClpP进行了结晶，并对上述数据进行了分析。 已经被用来帮助解决X射线结构。 数个半胱氨酸 突变体被工程化和Au标记，并在STEK中进行检查，以帮助 在结构的确定上。 CIpA已在 茎 初步的样品不是很好，但进一步的尝试 更好的净化样本正在进行中 ClpA组分可以是 六聚体 最后的目标是研究ClpP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.