Banner D W, Kokkinidis M, Tsernoglou D
EMBL, Heidelberg, FRG.
J Mol Biol. 1987 Aug 5;196(3):657-75. doi: 10.1016/0022-2836(87)90039-8.
Structural details of the Rop protein from plasmid ColE1 are presented, with a description of the X-ray crystal structure determination and refinement at a nominal resolution of 1.7 A. The 63 amino acid protein is a dimer. Each monomer consists almost entirely of two alpha helices, the whole molecule forming a highly regular four-alpha-helix bundle. This may be approximated by a four-stranded rope with a radius of 7.0 A, a left-handed helical twist and a pitch of 172.5 A. The packing constraints for this novel type of coiled-coil structure are given. The protein acts in the control of plasmid replication via regulation of an RNA-RNA interaction in a manner not yet understood in atomic detail.
本文介绍了来自质粒ColE1的Rop蛋白的结构细节，并描述了在标称分辨率为1.7埃下的X射线晶体结构测定和精修过程。该63个氨基酸的蛋白为二聚体。每个单体几乎完全由两个α螺旋组成，整个分子形成高度规则的四α螺旋束。这可以近似为半径为7.0埃、左旋螺旋扭曲且螺距为172.5埃的四链绳索。给出了这种新型卷曲螺旋结构的堆积限制。该蛋白通过调控一种尚未在原子细节上理解的RNA-RNA相互作用来控制质粒复制。
