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1co4

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(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="450" color="white" frame="true" align="right" spinBox="true"
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[[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==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CO4 OCA].
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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]]
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[[Category: Posewitz, M.C.]]
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[[Category: Posewitz, M C.]]
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[[Category: Smith, D.L.]]
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[[Category: Smith, D L.]]
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[[Category: Summers, M.F.]]
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[[Category: Summers, M F.]]
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[[Category: Turner, R.B.]]
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[[Category: Turner, R B.]]
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[[Category: Winge, D.R.]]
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[[Category: Winge, D R.]]
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[[Category: Zawrotny, M.E.]]
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[[Category: Zawrotny, M E.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: amt]]
[[Category: amt]]
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[[Category: metallothionein]]
[[Category: metallothionein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:36:52 2007''
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''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


1co4

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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

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