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Title
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Structure of the ColE1 rop protein at 1.7 A resolution.
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Authors
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D.W.Banner,
M.Kokkinidis,
D.Tsernoglou.
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Ref.
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J Mol Biol, 1987,
196,
657-675.
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PubMed id
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Abstract
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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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