1co4
From Proteopedia
(New page: 200px<br /><applet load="1co4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1co4" /> '''SOLUTION STRUCTURE OF A ZINC DOMAIN CONSERVE...) |
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| - | [[Image:1co4.gif|left|200px]]<br /><applet load="1co4" size=" | + | [[Image:1co4.gif|left|200px]]<br /><applet load="1co4" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1co4" /> | caption="1co4" /> | ||
'''SOLUTION STRUCTURE OF A ZINC DOMAIN CONSERVED IN YEAST COPPER-REGULATED TRANSCRIPTION FACTORS'''<br /> | '''SOLUTION STRUCTURE OF A ZINC DOMAIN CONSERVED IN YEAST COPPER-REGULATED TRANSCRIPTION FACTORS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three dimensional structure of the N-terminal domain (residues 1-42) | + | The three dimensional structure of the N-terminal domain (residues 1-42) of the copper-responsive transcription factor Amtl from Candida glabrata has been determined by two-dimensional 1H-correlated nuclear magnetic resonance (NMR) methods. The domain contains an array of zinc-binding residues (Cys-X2-Cys-X8-Cys-X-His) that is conserved among a family of Cu-responsive transcription factors. The structure is unlike those of previously characterized zinc finger motifs, and consists of a three-stranded antiparallel beta-sheet with two short helical segments that project from one end of the beta-sheet. Conserved residues at positions 16, 18 and 19 form a basic patch that may be important for DNA binding. |
==About this Structure== | ==About this Structure== | ||
| - | 1CO4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1CO4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] 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=1CO4 OCA]. |
==Reference== | ==Reference== | ||
Solution structure of a zinc domain conserved in yeast copper-regulated transcription factors., Turner RB, Smith DL, Zawrotny ME, Summers MF, Posewitz MC, Winge DR, Nat Struct Biol. 1998 Jul;5(7):551-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9665167 9665167] | Solution structure of a zinc domain conserved in yeast copper-regulated transcription factors., Turner RB, Smith DL, Zawrotny ME, Summers MF, Posewitz MC, Winge DR, Nat Struct Biol. 1998 Jul;5(7):551-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9665167 9665167] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Posewitz, M | + | [[Category: Posewitz, M C.]] |
| - | [[Category: Smith, D | + | [[Category: Smith, D L.]] |
| - | [[Category: Summers, M | + | [[Category: Summers, M F.]] |
| - | [[Category: Turner, R | + | [[Category: Turner, R B.]] |
| - | [[Category: Winge, D | + | [[Category: Winge, D R.]] |
| - | [[Category: Zawrotny, M | + | [[Category: Zawrotny, M E.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: amt]] | [[Category: amt]] | ||
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[[Category: metallothionein]] | [[Category: metallothionein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:07:58 2008'' |
Revision as of 10:08, 21 February 2008
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SOLUTION STRUCTURE OF A ZINC DOMAIN CONSERVED IN YEAST COPPER-REGULATED TRANSCRIPTION FACTORS
Overview
The three dimensional structure of the N-terminal domain (residues 1-42) of the copper-responsive transcription factor Amtl from Candida glabrata has been determined by two-dimensional 1H-correlated nuclear magnetic resonance (NMR) methods. The domain contains an array of zinc-binding residues (Cys-X2-Cys-X8-Cys-X-His) that is conserved among a family of Cu-responsive transcription factors. The structure is unlike those of previously characterized zinc finger motifs, and consists of a three-stranded antiparallel beta-sheet with two short helical segments that project from one end of the beta-sheet. Conserved residues at positions 16, 18 and 19 form a basic patch that may be important for DNA binding.
About this Structure
1CO4 is a Single protein structure of sequence from [1] with as ligand. Full crystallographic information is available from OCA.
Reference
Solution structure of a zinc domain conserved in yeast copper-regulated transcription factors., Turner RB, Smith DL, Zawrotny ME, Summers MF, Posewitz MC, Winge DR, Nat Struct Biol. 1998 Jul;5(7):551-5. PMID:9665167
Page seeded by OCA on Thu Feb 21 12:07:58 2008
