Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
复制标题
DOI：
10.1126/science.276.5311.431
复制
发表时间：
1997-04-18
期刊：
影响因子：
56.9
通讯作者：
Kuriyan, J
中科院分区：
文献类型：
--
作者：
Harrison, CJ;HayerHartl, M;Kuriyan, J
在2.8埃分辨率下测定了大肠杆菌DnaK[热休克蛋白70 (Hsp70)]中腺嘌呤核苷酸交换因子GrpE与腺苷三磷酸酶（ATPase）结构域复合物的晶体结构。GrpE二聚体不对称地与dna的单个分子结合。与GrpE复合物的无核苷酸atp酶结构域的结构与核苷酸结合的哺乳动物Hsp70同源物非常相似，除了蛋白质的一个亚结构域向外旋转。这种构象变化与核苷酸紧密结合不一致。两个长α螺旋从GrpE二聚体延伸出来，表明GrpE在DnaK肽释放中的作用。
The crystal structure of the adenine nucleotide exchange factor GrpE in complex with the adenosine triphosphatase (ATPase) domain of Escherichia coli DnaK [heat shock protein 70 (Hsp70)] was determined at 2.8 angstrom resolution. A dimer of GrpE binds asymmetrically to a single molecule of DnaK. The structure of the nucleotide-free ATPase domain in complex with GrpE resembles closely that of the nucleotide-bound mammalian Hsp70 homolog, except for an outward rotation of one of the subdomains of the protein. This conformational change is not consistent with tight nucleotide binding. Two long alpha helices extend away from the GrpE dimer and suggest a role for GrpE in peptide release from DnaK.