1yfb: Difference between revisions

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

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

caption="1yfb" />

'''The solution structure of the N-domain of the transcription factor abrB'''<br />

==Overview==

AbrB is a key transition-state regulator of Bacillus subtilis. Based on, the conservation of a betaalphabeta structural unit, we proposed a beta, barrel fold for its DNA binding domain, similar to, but topologically, distinct from, double-psi beta barrels. However, the NMR structure, revealed a novel fold, the "looped-hinge helix." To understand this, discrepancy, we undertook a bioinformatics study of AbrB and its homologs;, these form a large superfamily, which includes SpoVT, PrlF, MraZ, addiction module antidotes (PemI, MazE), plasmid maintenance proteins, (VagC, VapB), and archaeal PhoU homologs. MazE and MraZ form, swapped-hairpin beta barrels. We therefore reexamined the fold of AbrB by, NMR spectroscopy and found that it also forms a swapped-hairpin barrel., The conservation of the core betaalphabeta element supports a common, evolutionary origin for swapped-hairpin and double-psi barrels, which we, group into a higher-order class, the cradle-loop barrels, based on the, peculiar shape of their ligand binding site.

AbrB is a key transition-state regulator of Bacillus subtilis. Based on the conservation of a betaalphabeta structural unit, we proposed a beta barrel fold for its DNA binding domain, similar to, but topologically distinct from, double-psi beta barrels. However, the NMR structure revealed a novel fold, the "looped-hinge helix." To understand this discrepancy, we undertook a bioinformatics study of AbrB and its homologs; these form a large superfamily, which includes SpoVT, PrlF, MraZ, addiction module antidotes (PemI, MazE), plasmid maintenance proteins (VagC, VapB), and archaeal PhoU homologs. MazE and MraZ form swapped-hairpin beta barrels. We therefore reexamined the fold of AbrB by NMR spectroscopy and found that it also forms a swapped-hairpin barrel. The conservation of the core betaalphabeta element supports a common evolutionary origin for swapped-hairpin and double-psi barrels, which we group into a higher-order class, the cradle-loop barrels, based on the peculiar shape of their ligand binding site.

==About this Structure==

1YFB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1YFB OCA].

1YFB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YFB OCA].

==Reference==

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[[Category: nmr; homodimer; bioinformatics; swapped-hairpin barrel]]

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@@ Line 1: / Line 1: @@
-[[Image:1yfb.jpg|left|200px]]<br /><applet load="1yfb" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1yfb.jpg|left|200px]]<br /><applet load="1yfb" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1yfb" />
 '''The solution structure of the N-domain of the transcription factor abrB'''<br />
 ==Overview==
-AbrB is a key transition-state regulator of Bacillus subtilis. Based on, the conservation of a betaalphabeta structural unit, we proposed a beta, barrel fold for its DNA binding domain, similar to, but topologically, distinct from, double-psi beta barrels. However, the NMR structure, revealed a novel fold, the "looped-hinge helix." To understand this, discrepancy, we undertook a bioinformatics study of AbrB and its homologs;, these form a large superfamily, which includes SpoVT, PrlF, MraZ, addiction module antidotes (PemI, MazE), plasmid maintenance proteins, (VagC, VapB), and archaeal PhoU homologs. MazE and MraZ form, swapped-hairpin beta barrels. We therefore reexamined the fold of AbrB by, NMR spectroscopy and found that it also forms a swapped-hairpin barrel., The conservation of the core betaalphabeta element supports a common, evolutionary origin for swapped-hairpin and double-psi barrels, which we, group into a higher-order class, the cradle-loop barrels, based on the, peculiar shape of their ligand binding site.
+AbrB is a key transition-state regulator of Bacillus subtilis. Based on the conservation of a betaalphabeta structural unit, we proposed a beta barrel fold for its DNA binding domain, similar to, but topologically distinct from, double-psi beta barrels. However, the NMR structure revealed a novel fold, the "looped-hinge helix." To understand this discrepancy, we undertook a bioinformatics study of AbrB and its homologs; these form a large superfamily, which includes SpoVT, PrlF, MraZ, addiction module antidotes (PemI, MazE), plasmid maintenance proteins (VagC, VapB), and archaeal PhoU homologs. MazE and MraZ form swapped-hairpin beta barrels. We therefore reexamined the fold of AbrB by NMR spectroscopy and found that it also forms a swapped-hairpin barrel. The conservation of the core betaalphabeta element supports a common evolutionary origin for swapped-hairpin and double-psi barrels, which we group into a higher-order class, the cradle-loop barrels, based on the peculiar shape of their ligand binding site.
 ==About this Structure==
-YFB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YFB OCA].
+YFB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YFB OCA].
 ==Reference==
@@ Line 18: / Line 18: @@
 [[Category: nmr; homodimer; bioinformatics; swapped-hairpin barrel]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:43:58 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:04:45 2008''