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2ere
From Proteopedia
(New page: 200px<br /><applet load="2ere" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ere, resolution 3.00Å" /> '''Crystal Structure of...) |
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| - | [[Image:2ere.gif|left|200px]]<br /><applet load="2ere" size=" | + | [[Image:2ere.gif|left|200px]]<br /><applet load="2ere" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ere, resolution 3.00Å" /> | caption="2ere, resolution 3.00Å" /> | ||
'''Crystal Structure of a Leu3 DNA-binding domain complexed with a 15mer DNA duplex'''<br /> | '''Crystal Structure of a Leu3 DNA-binding domain complexed with a 15mer DNA duplex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Gal4 is the prototypical Zn2Cys6 binuclear cluster transcriptional | + | 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== | ||
| - | 2ERE 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:// | + | 2ERE 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=2ERE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Fitzgerald, M | + | [[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:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:13:47 2008'' |
Revision as of 15:13, 21 February 2008
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Crystal Structure of a Leu3 DNA-binding domain complexed with a 15mer 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
2ERE 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 17:13:47 2008
