1ROP

STRUCTURE OF THE COL*E1 ROP PROTEIN AT 1.7 ANGSTROMS RESOLUTION

Summary for 1ROP

• Entry DOI: 10.2210/pdb1rop/pdb
• Descriptor: ROP PROTEIN (2 entities in total)
• Functional Keywords: transcription regulation
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 7237.04

Authors

Kokkinidis, M.,Banner, D.W.,Tsernoglou, D. (deposition date: 1991-04-02, release date: 1992-07-15, Last modification date: 2024-02-14)

Primary citation

Banner, D.W.,Kokkinidis, M.,Tsernoglou, D.
Structure of the ColE1 rop protein at 1.7 A resolution
J.Mol.Biol., 196:657-675, 1987

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.

PubMed: 3681971
DOI: 10.1016/0022-2836(87)90039-8

Experimental method

X-RAY DIFFRACTION (1.7 Å)