1F36

THE CRYSTAL STRUCTURE OF FIS MUTANT K36E REVEALS THAT THE TRANSACTIVATION REGION OF THE FIS PROTEIN CONTAINS EXTENDED MOBILE BETA-HAIRPIN ARMS

Summary for 1F36

• Entry DOI: 10.2210/pdb1f36/pdb
• Descriptor: FIS (2 entities in total)
• Functional Keywords: transactivation region, dna-binding protein, protein-protein interaction domain
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 22505.71

Authors

Safo, M.K.,Yuan, H.S. (deposition date: 1997-06-20, release date: 1997-12-24, Last modification date: 2024-04-03)

Primary citation

Safo, M.K.,Yang, W.Z.,Corselli, L.,Cramton, S.E.,Yuan, H.S.,Johnson, R.C.
The transactivation region of the fis protein that controls site-specific DNA inversion contains extended mobile beta-hairpin arms.
EMBO J., 16:6860-6873, 1997

PubMed Abstract: 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.

PubMed: 9362499
DOI: 10.1093/emboj/16.22.6860

Experimental method

X-RAY DIFFRACTION (2.65 Å)