1ROP

Structure of the ColE1 rop protein at 1.7 A resolution

(1987) J Mol Biol 196: 657-675

• PubMed: 3681971 Search on PubMed
• DOI: https://doi.org/10.1016/0022-2836(87)90039-8
• Primary Citation of Related Structures:  
  1ROP


• PubMed Abstract: 
  

  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.

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Organizational Affiliation: 

EMBL, Heidelberg, FRG.