A corrected quaternary arrangement of the peptidase HslV and atpase HslU in a cocrystal structure.
A corrected quaternary arrangement of the peptidase HslV and atpase HslU in a cocrystal structure.
复制标题
共晶结构中肽酶 HslV 和 atpase HslU 的正确四级排列。
DOI：
10.1006/jsbi.2001.4347
复制
发表时间：
2001
影响因子：
3
通讯作者：
J. Wang
中科院分区：
文献类型：
--
作者：
J. Wang
细菌热休克基因座HslU ATP酶和HslV肽酶一起形成ATP依赖性HslVU蛋白酶。晶体结构显示HslU形成在一端具有孔的六聚体，HslV形成在两个背靠背堆叠的六聚体环的两端具有易位孔的十二聚体。与三个电子显微镜研究和一个小角X-射线散射研究一致，三个晶体结构显示HslU的核苷酸结合结构域与HslV结合，并且肽酶和ATP酶的孔彼此相邻并对齐。第四种晶体结构显示出完全不同的四元排列。在这里，我提出了一个晶体学分析的第四个结构，以表明它包含了一个晶体学的起源移动和错误的空间群分配。一旦这些错误被纠正，一个四元排列，这是类似于在其他结构中观察到的出现。
The bacterial heat shock locus HslU ATPase and HslV peptidase together form an ATP-dependent HslVU protease. Crystal structures show that HslU forms a hexamer with a pore at one end and HslV forms a dodecamer with translocation pores at both ends of two back-to-back stacked hexameric rings. Consistent with three electron microscopic studies and one small-angle X-ray scattering study, three crystal structures show that the nucleotide-binding domains of HslU bind to HslV and that the pores of the peptidase and ATPase are next to each other and aligned. A fourth crystal structure shows a radically different quaternary arrangement. Here I present a crystallographic analysis of the fourth structure to show that it contained a crystallographic origin shift and a mistake in space group assignment. Once these errors are corrected, a quaternary arrangement that is similar to those observed in the other structures emerges.
影响因子：
56.9
作者：
Luecke, H;Richter, HT;Lanyi, JK
通讯作者：
Lanyi, JK
DOI：
10.1073/pnas.93.12.5808
发表时间：
1996-06-11
影响因子：
11.1
作者：
Rohrwild, M;Coux, O;Goldberg, AL
通讯作者：
Goldberg, AL