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Structure of the ColE1 Rop protein at 1.7 Å resolution

1987; Elsevier BV; Volume: 196; Issue: 3 Linguagem: Inglês

10.1016/0022-2836(87)90039-8

1089-8638

David W. Banner, Michael Kokkinidis, Demetrius Tsernoglou,

Enzyme Structure and Function

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 Å. 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 Å, a left-handed helical twist and a pitch of 172.5 Å. 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.