1f36
From Proteopedia
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THE CRYSTAL STRUCTURE OF FIS MUTANT K36E REVEALS THAT THE TRANSACTIVATION REGION OF THE FIS PROTEIN CONTAINS EXTENDED MOBILE BETA-HAIRPIN ARMS
Overview
The Fis protein regulates site-specific DNA inversion catalyzed by a family of DNA invertases when bound to a cis-acting recombinational enhancer. As is often found for transactivation domains, previous crystal structures have failed to resolve the conformation of the N-terminal inversion activation region within the Fis dimer. A new crystal form of a mutant Fis protein now reveals that the activation region contains two beta-hairpin arms that protrude over 20 A from the protein core. Saturation mutagenesis identified the regulatory and structurally important amino acids. The most critical activating residues are located near the tips of the beta-arms. Disulfide cross-linking between the beta-arms demonstrated that they are highly flexible in solution and that efficient inversion activation can occur when the beta-arms are covalently linked together. The emerging picture for this regulatory motif is that contacts with the recombinase at the tip of the mobile beta-arms activate the DNA invertase in the context of an invertasome complex.
About this Structure
1F36 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The transactivation region of the fis protein that controls site-specific DNA inversion contains extended mobile beta-hairpin arms., Safo MK, Yang WZ, Corselli L, Cramton SE, Yuan HS, Johnson RC, EMBO J. 1997 Nov 17;16(22):6860-73. PMID:9362499
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