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J Mol Biol. 1987 Aug 5;196(3):657-75.

Structure of the ColE1 rop protein at 1.7 A resolution.

Author information

1
EMBL, Heidelberg, FRG.

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.

PMID:
3681971
DOI:
10.1016/0022-2836(87)90039-8
[Indexed for MEDLINE]

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