1f36: Difference between revisions
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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''' | {{Structure | ||
|PDB= 1f36 |SIZE=350|CAPTION= <scene name='initialview01'>1f36</scene>, resolution 2.65Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= FIS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''THE CRYSTAL STRUCTURE OF FIS MUTANT K36E REVEALS THAT THE TRANSACTIVATION REGION OF THE FIS PROTEIN CONTAINS EXTENDED MOBILE BETA-HAIRPIN ARMS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1F36 is a [ | 1F36 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F36 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9362499 9362499] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transactivation region]] | [[Category: transactivation region]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:03:44 2008'' | ||
Revision as of 09:03, 20 March 2008
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| 1f36, resolution 2.65Å | |||||||||||||
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| Gene: | FIS (Escherichia coli) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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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