1f36: Difference between revisions

Line 1:

[[Image:1f36.jpg|left|200px]]<br /><applet load="1f36" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1f36.jpg|left|200px]]<br /><applet load="1f36" size="350" color="white" frame="true" align="right" spinBox="true"

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 />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1F36 OCA].

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==

Line 13:

[[Category: Escherichia coli]]

[[Category: Single protein]]

[[Category: Safo, M.K.]]

[[Category: Safo, M K.]]

[[Category: Yuan, H.S.]]

[[Category: Yuan, H S.]]

[[Category: dna-binding protein]]

[[Category: protein-protein interaction domain]]

[[Category: transactivation region]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 14~~:34:~~10 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:18 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1f36.jpg|left|200px]]<br /><applet load="1f36" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1f36.jpg|left|200px]]<br /><applet load="1f36" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1f36, resolution 2.65&Aring;" />
 '''THE CRYSTAL STRUCTURE OF FIS MUTANT K36E REVEALS THAT THE TRANSACTIVATION REGION OF THE FIS PROTEIN CONTAINS EXTENDED MOBILE BETA-HAIRPIN ARMS'''<br />
 ==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.
+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==
-F36 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F36 OCA].
+F36 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==
@@ Line 13: / Line 13: @@
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Safo, M.K.]]
+[[Category: Safo, M K.]]
-[[Category: Yuan, H.S.]]
+[[Category: Yuan, H S.]]
 [[Category: dna-binding protein]]
 [[Category: protein-protein interaction domain]]
 [[Category: transactivation region]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:34:10 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:18 2008''