1f36
From Proteopedia
(New page: 200px<br /><applet load="1f36" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f36, resolution 2.65Å" /> '''THE CRYSTAL STRUCTUR...) |
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| - | [[Image:1f36.jpg|left|200px]]<br /><applet load="1f36" size=" | + | [[Image:1f36.jpg|left|200px]]<br /><applet load="1f36" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1f36, resolution 2.65Å" /> | caption="1f36, resolution 2.65Å" /> | ||
'''THE CRYSTAL STRUCTURE OF FIS MUTANT K36E REVEALS THAT THE TRANSACTIVATION REGION OF THE FIS PROTEIN CONTAINS EXTENDED MOBILE BETA-HAIRPIN ARMS'''<br /> | '''THE CRYSTAL STRUCTURE OF FIS MUTANT K36E REVEALS THAT THE TRANSACTIVATION REGION OF THE FIS PROTEIN CONTAINS EXTENDED MOBILE BETA-HAIRPIN ARMS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Fis protein regulates site-specific DNA inversion catalyzed by a | + | 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== | ==About this Structure== | ||
| - | 1F36 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1F36 is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Safo, M | + | [[Category: Safo, M K.]] |
| - | [[Category: Yuan, H | + | [[Category: Yuan, H S.]] |
[[Category: dna-binding protein]] | [[Category: dna-binding protein]] | ||
[[Category: protein-protein interaction domain]] | [[Category: protein-protein interaction domain]] | ||
[[Category: transactivation region]] | [[Category: transactivation region]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:18 2008'' |
Revision as of 10:34, 21 February 2008
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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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