2erg: Difference between revisions

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

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

caption="2erg, resolution 3.15Å" />

'''Crystal Structure of Leu3 DNA-binding domain with a single H50C mutation complexed with a 15mer DNA duplex'''<br />

==Overview==

Gal4 is the prototypical Zn2Cys6 binuclear cluster transcriptional, regulator that binds as a homodimer to DNA containing inverted CGG, half-sites. Leu3, a member of this protein family, binds to everted, (opposite polarity to inverted) CGG half-sites, and an H50C mutation, within the Leu3 Zn2Cys6 binuclear motif abolishes its transcriptional, repression function without impairing DNA binding. We report the X-ray, crystal structures of DNA complexes with Leu3 and Leu3(H50C) and solution, DNA binding studies of selected Leu3 mutant proteins. These studies reveal, the molecular details of everted CGG half-site recognition, and suggest a, role for the H50C mutation in transcriptional repression. Comparison with, the Gal4-DNA complex shows an unexpected conservation in the DNA, recognition mode of inverted and everted CGG half-sites, and points to a, critical function of a linker region between the Zn2Cys6 binuclear cluster, and dimerization regions in DNA binding specificity. Broader implications, of these findings are discussed.

Gal4 is the prototypical Zn2Cys6 binuclear cluster transcriptional regulator that binds as a homodimer to DNA containing inverted CGG half-sites. Leu3, a member of this protein family, binds to everted (opposite polarity to inverted) CGG half-sites, and an H50C mutation within the Leu3 Zn2Cys6 binuclear motif abolishes its transcriptional repression function without impairing DNA binding. We report the X-ray crystal structures of DNA complexes with Leu3 and Leu3(H50C) and solution DNA binding studies of selected Leu3 mutant proteins. These studies reveal the molecular details of everted CGG half-site recognition, and suggest a role for the H50C mutation in transcriptional repression. Comparison with the Gal4-DNA complex shows an unexpected conservation in the DNA recognition mode of inverted and everted CGG half-sites, and points to a critical function of a linker region between the Zn2Cys6 binuclear cluster and dimerization regions in DNA binding specificity. Broader implications of these findings are discussed.

==About this Structure==

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

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

==Reference==

Line 13:

[[Category: Saccharomyces cerevisiae]]

[[Category: Single protein]]

[[Category: Fitzgerald, M.X.]]

[[Category: Fitzgerald, M X.]]

[[Category: Marmorstein, R.]]

[[Category: ZN]]

[[Category: zn(2)cys(6) binuclear cluster motif]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 10:06:~~16 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:13:47 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2erg.gif|left|200px]]<br /><applet load="2erg" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2erg.gif|left|200px]]<br /><applet load="2erg" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2erg, resolution 3.15&Aring;" />
 '''Crystal Structure of Leu3 DNA-binding domain with a single H50C mutation complexed with a 15mer DNA duplex'''<br />
 ==Overview==
-Gal4 is the prototypical Zn2Cys6 binuclear cluster transcriptional, regulator that binds as a homodimer to DNA containing inverted CGG, half-sites. Leu3, a member of this protein family, binds to everted, (opposite polarity to inverted) CGG half-sites, and an H50C mutation, within the Leu3 Zn2Cys6 binuclear motif abolishes its transcriptional, repression function without impairing DNA binding. We report the X-ray, crystal structures of DNA complexes with Leu3 and Leu3(H50C) and solution, DNA binding studies of selected Leu3 mutant proteins. These studies reveal, the molecular details of everted CGG half-site recognition, and suggest a, role for the H50C mutation in transcriptional repression. Comparison with, the Gal4-DNA complex shows an unexpected conservation in the DNA, recognition mode of inverted and everted CGG half-sites, and points to a, critical function of a linker region between the Zn2Cys6 binuclear cluster, and dimerization regions in DNA binding specificity. Broader implications, of these findings are discussed.
+Gal4 is the prototypical Zn2Cys6 binuclear cluster transcriptional regulator that binds as a homodimer to DNA containing inverted CGG half-sites. Leu3, a member of this protein family, binds to everted (opposite polarity to inverted) CGG half-sites, and an H50C mutation within the Leu3 Zn2Cys6 binuclear motif abolishes its transcriptional repression function without impairing DNA binding. We report the X-ray crystal structures of DNA complexes with Leu3 and Leu3(H50C) and solution DNA binding studies of selected Leu3 mutant proteins. These studies reveal the molecular details of everted CGG half-site recognition, and suggest a role for the H50C mutation in transcriptional repression. Comparison with the Gal4-DNA complex shows an unexpected conservation in the DNA recognition mode of inverted and everted CGG half-sites, and points to a critical function of a linker region between the Zn2Cys6 binuclear cluster and dimerization regions in DNA binding specificity. Broader implications of these findings are discussed.
 ==About this Structure==
-ERG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ERG OCA].
+ERG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ERG OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Saccharomyces cerevisiae]]
 [[Category: Single protein]]
-[[Category: Fitzgerald, M.X.]]
+[[Category: Fitzgerald, M X.]]
 [[Category: Marmorstein, R.]]
 [[Category: ZN]]
 [[Category: zn(2)cys(6) binuclear cluster motif]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:06:16 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:13:47 2008''