2hts: Difference between revisions

Line 1:

[[Image:2hts.gif|left|200px]]<br /><applet load="2hts" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2hts.gif|left|200px]]<br /><applet load="2hts" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2hts, resolution 1.83Å" />

'''CRYSTAL STRUCTURE OF THE DNA BINDING DOMAIN OF THE HEAT SHOCK TRANSCRIPTION FACTOR'''<br />

==Overview==

The structure of the DNA binding domain, determined at 1.8 angstrom, resolution, contains a three-helix bundle that is capped by a, four-stranded antiparallel beta sheet. This structure is a variant of the, helix-turn-helix motif, typified by catabolite activator protein. In the, heat shock transcription factor, the first helix of the motif (alpha 2), has an alpha-helical bulge and a proline-induced kink. The angle between, the two helices of the motif (alpha 2 and alpha 3) is about 20 degrees, smaller than the average for canonical helix-turn-helix proteins., Nevertheless, the relative positions of the first and third helices of the, bundle (alpha 1 and alpha 3) are conserved. It is proposed here that the, first helix of the three-helix bundle be considered a component of the, helix-turn-helix motif.

The structure of the DNA binding domain, determined at 1.8 angstrom resolution, contains a three-helix bundle that is capped by a four-stranded antiparallel beta sheet. This structure is a variant of the helix-turn-helix motif, typified by catabolite activator protein. In the heat shock transcription factor, the first helix of the motif (alpha 2) has an alpha-helical bulge and a proline-induced kink. The angle between the two helices of the motif (alpha 2 and alpha 3) is about 20 degrees smaller than the average for canonical helix-turn-helix proteins. Nevertheless, the relative positions of the first and third helices of the bundle (alpha 1 and alpha 3) are conserved. It is proposed here that the first helix of the three-helix bundle be considered a component of the helix-turn-helix motif.

==About this Structure==

2HTS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Kluyveromyces_lactis Kluyveromyces lactis] with ACY as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2HTS OCA].

2HTS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Kluyveromyces_lactis Kluyveromyces lactis] with <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HTS OCA].

==Reference==

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[[Category: transcription factor]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 11:58:~~44 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:45:38 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2hts.gif|left|200px]]<br /><applet load="2hts" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2hts.gif|left|200px]]<br /><applet load="2hts" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2hts, resolution 1.83&Aring;" />
 '''CRYSTAL STRUCTURE OF THE DNA BINDING DOMAIN OF THE HEAT SHOCK TRANSCRIPTION FACTOR'''<br />
 ==Overview==
-The structure of the DNA binding domain, determined at 1.8 angstrom, resolution, contains a three-helix bundle that is capped by a, four-stranded antiparallel beta sheet. This structure is a variant of the, helix-turn-helix motif, typified by catabolite activator protein. In the, heat shock transcription factor, the first helix of the motif (alpha 2), has an alpha-helical bulge and a proline-induced kink. The angle between, the two helices of the motif (alpha 2 and alpha 3) is about 20 degrees, smaller than the average for canonical helix-turn-helix proteins., Nevertheless, the relative positions of the first and third helices of the, bundle (alpha 1 and alpha 3) are conserved. It is proposed here that the, first helix of the three-helix bundle be considered a component of the, helix-turn-helix motif.
+The structure of the DNA binding domain, determined at 1.8 angstrom resolution, contains a three-helix bundle that is capped by a four-stranded antiparallel beta sheet. This structure is a variant of the helix-turn-helix motif, typified by catabolite activator protein. In the heat shock transcription factor, the first helix of the motif (alpha 2) has an alpha-helical bulge and a proline-induced kink. The angle between the two helices of the motif (alpha 2 and alpha 3) is about 20 degrees smaller than the average for canonical helix-turn-helix proteins. Nevertheless, the relative positions of the first and third helices of the bundle (alpha 1 and alpha 3) are conserved. It is proposed here that the first helix of the three-helix bundle be considered a component of the helix-turn-helix motif.
 ==About this Structure==
-HTS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Kluyveromyces_lactis Kluyveromyces lactis] with ACY as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HTS OCA].
+HTS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Kluyveromyces_lactis Kluyveromyces lactis] with <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HTS OCA].
 ==Reference==
@@ Line 18: / Line 18: @@
 [[Category: transcription factor]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:58:44 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:45:38 2008''