2er8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2er8" size="450" color="white" frame="true" align="right" spinBox="true" caption="2er8, resolution 2.85&Aring;" /> '''Crystal Structure of...)
Line 1: Line 1:
-
[[Image:2er8.gif|left|200px]]<br /><applet load="2er8" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2er8.gif|left|200px]]<br /><applet load="2er8" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2er8, resolution 2.85&Aring;" />
caption="2er8, resolution 2.85&Aring;" />
'''Crystal Structure of Leu3 DNA-binding domain complexed with a 12mer DNA duplex'''<br />
'''Crystal Structure of Leu3 DNA-binding domain complexed with a 12mer DNA duplex'''<br />
==Overview==
==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==
==About this Structure==
-
2ER8 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=2ER8 OCA].
+
2ER8 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=2ER8 OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Fitzgerald, M.X.]]
+
[[Category: Fitzgerald, M X.]]
[[Category: Marmorstein, R.]]
[[Category: Marmorstein, R.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: zn(2)cys(6) binuclear cluster motif]]
[[Category: zn(2)cys(6) binuclear cluster motif]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:05:54 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:13:44 2008''

Revision as of 15:13, 21 February 2008


2er8, resolution 2.85Å

Drag the structure with the mouse to rotate

Crystal Structure of Leu3 DNA-binding domain complexed with a 12mer DNA duplex

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.

About this Structure

2ER8 is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of a Leu3-DNA complex: recognition of everted CGG half-sites by a Zn2Cys6 binuclear cluster protein., Fitzgerald MX, Rojas JR, Kim JM, Kohlhaw GB, Marmorstein R, Structure. 2006 Apr;14(4):725-35. PMID:16615914

Page seeded by OCA on Thu Feb 21 17:13:44 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools