Allen Mark D, Buckle Ashley M, Cordell Suzanne C, Löwe Jan, Bycroft Mark
MRC Centre for Protein Engineering, and Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
J Mol Biol. 2003 Jul 11;330(3):503-11. doi: 10.1016/s0022-2836(03)00473-x.
MacroH2A is an unusual histone H2A variant that has an extensive C-terminal tail that comprises approximately two thirds of the protein. The C-terminal non-histone domain of macroH2A is also found in a number of other proteins and has been termed the macro domain. Here we report the crystal structure to 1.7A of AF1521, a protein consisting of a stand-alone macro domain from Archaeoglobus fulgidus. The structure has a mixed alpha/beta fold that closely resembles the N-terminal DNA binding domain of the Escherichia coli leucine aminopeptidase PepA. The structure also shows some similarity to members of the P-loop family of nucleotide hydrolases.
巨核组蛋白H2A是一种不同寻常的组蛋白H2A变体，它有一个很长的C末端尾巴，约占该蛋白质的三分之二。巨核组蛋白H2A的C末端非组蛋白结构域也存在于许多其他蛋白质中，被称为巨结构域。在此我们报告嗜热栖热菌AF1521蛋白（由来自嗜热栖热菌的一个独立巨结构域组成）分辨率为1.7埃的晶体结构。该结构具有混合的α/β折叠，与大肠杆菌亮氨酸氨肽酶PepA的N末端DNA结合结构域极为相似。该结构也与核苷酸水解酶的P环家族成员有一些相似之处。
