STRUCTURE OF THE CO1E1 ROP PROTEIN AT 1.7 A RESOLUTION
STRUCTURE OF THE CO1E1 ROP PROTEIN AT 1.7 A RESOLUTION
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DOI：
10.1016/0022-2836(87)90039-8
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发表时间：
1987-08-05
影响因子：
5.6
通讯作者：
TSERNOGLOU, D
中科院分区：
文献类型：
--
作者：
BANNER, DW;KOKKINIDIS, M;TSERNOGLOU, D
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 .ANG.. 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 bundles. This may be approximated by a four-stranded rope with a radius of 7.0 .ANG., a left-handed helical twist and a pitch of 172.5 .ANG.. 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.
