1chc
From Proteopedia
(New page: 200px<br /><applet load="1chc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1chc" /> '''STRUCTURE OF THE C3HC4 DOMAIN BY 1H-NUCLEAR ...) |
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| - | [[Image:1chc.gif|left|200px]]<br /><applet load="1chc" size=" | + | [[Image:1chc.gif|left|200px]]<br /><applet load="1chc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1chc" /> | caption="1chc" /> | ||
'''STRUCTURE OF THE C3HC4 DOMAIN BY 1H-NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; A NEW STRUCTURAL CLASS OF ZINC-FINGER'''<br /> | '''STRUCTURE OF THE C3HC4 DOMAIN BY 1H-NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; A NEW STRUCTURAL CLASS OF ZINC-FINGER'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A recently identified sequence motif, referred to as "C3HC4" (also "RING | + | A recently identified sequence motif, referred to as "C3HC4" (also "RING finger" and "A Box") for its distinctive pattern of putative metal-binding residues, has been found in a wide range of proteins. In a previous paper we described the expression and purification of fragments encompassing this motif from the Vmw110 (IPC0) protein family. We showed that the equine herpes virus protein binds zinc ions and adopts a beta beta alpha beta fold. We now report the tertiary structure of this domain in solution, as determined by two-dimensional 1H-NMR An amphipathic alpha-helix lies along one surface of a triple-stranded beta-sheet. Four pairs of metal-binding residues sequester two zincs at distinct tetrahedral sites. The first and third pairs bind one metal ion, while the second and fourth pairs bind the other, forming an interleaved whole. The first and the fourth pairs are contained within two prominent, well-defined loops related by an approximate dyad symmetry. Conserved residues within the helix, sheet and loops contribute to a compact hydrophobic core. The region comprising the first two beta-strands and the alpha-helix has remarkable structural similarity with a TFIIIA type of zinc finger, even though the C3HC4 domain appears not to bind specifically to DNA or RNA. Using site-directed mutagenesis we demonstrate that exposed polar side-chains of the C3HC4 alpha-helix are essential for trans-activation of gene expression by an intact herpes virus regulatory protein. |
==About this Structure== | ==About this Structure== | ||
| - | 1CHC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equid_herpesvirus_3 Equid herpesvirus 3] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1CHC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equid_herpesvirus_3 Equid herpesvirus 3] 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=1CHC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Equid herpesvirus 3]] | [[Category: Equid herpesvirus 3]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Barlow, P | + | [[Category: Barlow, P N.]] |
| - | [[Category: Everett, R | + | [[Category: Everett, R D.]] |
[[Category: Luisi, B.]] | [[Category: Luisi, B.]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: viral protein]] | [[Category: viral protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:04 2008'' |
Revision as of 10:06, 21 February 2008
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STRUCTURE OF THE C3HC4 DOMAIN BY 1H-NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; A NEW STRUCTURAL CLASS OF ZINC-FINGER
Overview
A recently identified sequence motif, referred to as "C3HC4" (also "RING finger" and "A Box") for its distinctive pattern of putative metal-binding residues, has been found in a wide range of proteins. In a previous paper we described the expression and purification of fragments encompassing this motif from the Vmw110 (IPC0) protein family. We showed that the equine herpes virus protein binds zinc ions and adopts a beta beta alpha beta fold. We now report the tertiary structure of this domain in solution, as determined by two-dimensional 1H-NMR An amphipathic alpha-helix lies along one surface of a triple-stranded beta-sheet. Four pairs of metal-binding residues sequester two zincs at distinct tetrahedral sites. The first and third pairs bind one metal ion, while the second and fourth pairs bind the other, forming an interleaved whole. The first and the fourth pairs are contained within two prominent, well-defined loops related by an approximate dyad symmetry. Conserved residues within the helix, sheet and loops contribute to a compact hydrophobic core. The region comprising the first two beta-strands and the alpha-helix has remarkable structural similarity with a TFIIIA type of zinc finger, even though the C3HC4 domain appears not to bind specifically to DNA or RNA. Using site-directed mutagenesis we demonstrate that exposed polar side-chains of the C3HC4 alpha-helix are essential for trans-activation of gene expression by an intact herpes virus regulatory protein.
About this Structure
1CHC is a Single protein structure of sequence from Equid herpesvirus 3 with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the C3HC4 domain by 1H-nuclear magnetic resonance spectroscopy. A new structural class of zinc-finger., Barlow PN, Luisi B, Milner A, Elliott M, Everett R, J Mol Biol. 1994 Mar 25;237(2):201-11. PMID:8126734
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