1zme

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(New page: 200px<br /><applet load="1zme" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zme, resolution 2.5&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1zme.gif|left|200px]]<br /><applet load="1zme" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1zme, resolution 2.5&Aring;" />
caption="1zme, resolution 2.5&Aring;" />
'''CRYSTAL STRUCTURE OF PUT3/DNA COMPLEX'''<br />
'''CRYSTAL STRUCTURE OF PUT3/DNA COMPLEX'''<br />
==Overview==
==Overview==
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PUT3 is a member of a family of at least 79 fungal transcription factors, that contain a six-cysteine, two-zinc domain called a 'Zn2Cys6 binuclear, cluster'. We have determined the crystal structure of the DNA binding, region from the PUT3 protein bound to its cognate DNA target. The, structure reveals that the PUT3 homodimer is bound asymmetrically to the, DNA site. This asymmetry orients a beta-strand from one protein subunit, into the minor groove of the DNA resulting in a partial amino acid-base, pair intercalation and extensive direct and water-mediated protein, interactions with the minor groove of the DNA. These interactions, facilitate a sequence dependent kink at the centre of the DNA site and, specify the intervening base pairs separating two DNA half-sites that are, contacted in the DNA major groove. A comparison with the GAL4-DNA and, PPR1-DNA complexes shows how a family of related DNA binding proteins can, use a diverse set of mechanisms to discriminate between the base pairs, separating conserved DNA half-sites.
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PUT3 is a member of a family of at least 79 fungal transcription factors that contain a six-cysteine, two-zinc domain called a 'Zn2Cys6 binuclear cluster'. We have determined the crystal structure of the DNA binding region from the PUT3 protein bound to its cognate DNA target. The structure reveals that the PUT3 homodimer is bound asymmetrically to the DNA site. This asymmetry orients a beta-strand from one protein subunit into the minor groove of the DNA resulting in a partial amino acid-base pair intercalation and extensive direct and water-mediated protein interactions with the minor groove of the DNA. These interactions facilitate a sequence dependent kink at the centre of the DNA site and specify the intervening base pairs separating two DNA half-sites that are contacted in the DNA major groove. A comparison with the GAL4-DNA and PPR1-DNA complexes shows how a family of related DNA binding proteins can use a diverse set of mechanisms to discriminate between the base pairs separating conserved DNA half-sites.
==About this Structure==
==About this Structure==
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1ZME 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=1ZME OCA].
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1ZME 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=1ZME OCA].
==Reference==
==Reference==
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[[Category: zn2cys6]]
[[Category: zn2cys6]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:32:10 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:17:01 2008''

Revision as of 14:17, 21 February 2008


1zme, resolution 2.5Å

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CRYSTAL STRUCTURE OF PUT3/DNA COMPLEX

Overview

PUT3 is a member of a family of at least 79 fungal transcription factors that contain a six-cysteine, two-zinc domain called a 'Zn2Cys6 binuclear cluster'. We have determined the crystal structure of the DNA binding region from the PUT3 protein bound to its cognate DNA target. The structure reveals that the PUT3 homodimer is bound asymmetrically to the DNA site. This asymmetry orients a beta-strand from one protein subunit into the minor groove of the DNA resulting in a partial amino acid-base pair intercalation and extensive direct and water-mediated protein interactions with the minor groove of the DNA. These interactions facilitate a sequence dependent kink at the centre of the DNA site and specify the intervening base pairs separating two DNA half-sites that are contacted in the DNA major groove. A comparison with the GAL4-DNA and PPR1-DNA complexes shows how a family of related DNA binding proteins can use a diverse set of mechanisms to discriminate between the base pairs separating conserved DNA half-sites.

About this Structure

1ZME is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of a PUT3-DNA complex reveals a novel mechanism for DNA recognition by a protein containing a Zn2Cys6 binuclear cluster., Swaminathan K, Flynn P, Reece RJ, Marmorstein R, Nat Struct Biol. 1997 Sep;4(9):751-9. PMID:9303004

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