1f36

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[[Image:1f36.jpg|left|200px]]
[[Image:1f36.jpg|left|200px]]
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{{Structure
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|PDB= 1f36 |SIZE=350|CAPTION= <scene name='initialview01'>1f36</scene>, resolution 2.65&Aring;
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|GENE= FIS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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{{STRUCTURE_1f36| PDB=1f36 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f36 OCA], [http://www.ebi.ac.uk/pdbsum/1f36 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f36 RCSB]</span>
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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'''
'''THE CRYSTAL STRUCTURE OF FIS MUTANT K36E REVEALS THAT THE TRANSACTIVATION REGION OF THE FIS PROTEIN CONTAINS EXTENDED MOBILE BETA-HAIRPIN ARMS'''
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[[Category: Safo, M K.]]
[[Category: Safo, M K.]]
[[Category: Yuan, H S.]]
[[Category: Yuan, H S.]]
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[[Category: dna-binding protein]]
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[[Category: Dna-binding protein]]
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[[Category: protein-protein interaction domain]]
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[[Category: Protein-protein interaction domain]]
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[[Category: transactivation region]]
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[[Category: Transactivation region]]
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Revision as of 12:50, 2 May 2008

Template:STRUCTURE 1f36

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 Page seeded by OCA on Fri May 2 15:50:13 2008

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