1zfd
From Proteopedia
(New page: 200px<br /><applet load="1zfd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zfd" /> '''SWI5 ZINC FINGER DOMAIN 2, NMR, 45 STRUCTURE...) |
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| - | [[Image:1zfd.jpg|left|200px]]<br /><applet load="1zfd" size=" | + | [[Image:1zfd.jpg|left|200px]]<br /><applet load="1zfd" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1zfd" /> | caption="1zfd" /> | ||
'''SWI5 ZINC FINGER DOMAIN 2, NMR, 45 STRUCTURES'''<br /> | '''SWI5 ZINC FINGER DOMAIN 2, NMR, 45 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | This paper describes the detailed three-dimensional structures of two | + | This paper describes the detailed three-dimensional structures of two zinc-finger domains from the yeast transcription factor SWI5, calculated using the results of the n.m.r. experiments described in the accompanying paper. The structure of finger 2 is essentially similar to those previously obtained by others for isolated, synthetic single zinc-finger domains in solution, and for the three zinc-finger peptide Zif268 in its crystalline complex with DNA. The N-terminal half of the sequence forms a two-stranded, irregular beta-sheet containing both of the metal-binding cysteine residues, while the remainder of the structure forms a helix. Approximately the first half of this helix is alpha-helical, whereas the C-terminal portion, including the two metal-binding histidine residues, is 3(10) helical. Four invariant hydrophobic residues form a core to the structure. In contrast to all previously described structures of zinc-finger domains, finger 1 has an additional strand in the beta-sheet, formed by residues N-terminal to the formal start of the finger motif. This additional strand plays a role in stabilising the folded form of finger 1, since a two-finger peptide lacking the N-terminal residues showed folded structure in finger 2 but not in finger 1. |
==About this Structure== | ==About this Structure== | ||
| - | 1ZFD 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:// | + | 1ZFD 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=1ZFD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Neuhaus, D.]] | [[Category: Neuhaus, D.]] | ||
[[Category: Rhodes, D.]] | [[Category: Rhodes, D.]] | ||
| - | [[Category: Schwabe, J | + | [[Category: Schwabe, J W.R.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: dna binding motif]] | [[Category: dna binding motif]] | ||
[[Category: zinc finger dna binding domain]] | [[Category: zinc finger dna binding domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:14:59 2008'' |
Revision as of 14:15, 21 February 2008
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SWI5 ZINC FINGER DOMAIN 2, NMR, 45 STRUCTURES
Overview
This paper describes the detailed three-dimensional structures of two zinc-finger domains from the yeast transcription factor SWI5, calculated using the results of the n.m.r. experiments described in the accompanying paper. The structure of finger 2 is essentially similar to those previously obtained by others for isolated, synthetic single zinc-finger domains in solution, and for the three zinc-finger peptide Zif268 in its crystalline complex with DNA. The N-terminal half of the sequence forms a two-stranded, irregular beta-sheet containing both of the metal-binding cysteine residues, while the remainder of the structure forms a helix. Approximately the first half of this helix is alpha-helical, whereas the C-terminal portion, including the two metal-binding histidine residues, is 3(10) helical. Four invariant hydrophobic residues form a core to the structure. In contrast to all previously described structures of zinc-finger domains, finger 1 has an additional strand in the beta-sheet, formed by residues N-terminal to the formal start of the finger motif. This additional strand plays a role in stabilising the folded form of finger 1, since a two-finger peptide lacking the N-terminal residues showed folded structure in finger 2 but not in finger 1.
About this Structure
1ZFD is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.
Reference
Solution structures of two zinc-finger domains from SWI5 obtained using two-dimensional 1H nuclear magnetic resonance spectroscopy. A zinc-finger structure with a third strand of beta-sheet., Neuhaus D, Nakaseko Y, Schwabe JW, Klug A, J Mol Biol. 1992 Nov 20;228(2):637-51. PMID:1453468
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