1chc

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[[Image:1chc.gif|left|200px]]
 
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==STRUCTURE OF THE C3HC4 DOMAIN BY 1H-NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; A NEW STRUCTURAL CLASS OF ZINC-FINGER==
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The line below this paragraph, containing "STRUCTURE_1chc", creates the "Structure Box" on the page.
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<StructureSection load='1chc' size='340' side='right'caption='[[1chc]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1chc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equid_alphaherpesvirus_1 Equid alphaherpesvirus 1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CHC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CHC FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1chc| PDB=1chc | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1chc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1chc OCA], [https://pdbe.org/1chc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1chc RCSB], [https://www.ebi.ac.uk/pdbsum/1chc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1chc ProSAT]</span></td></tr>
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</table>
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'''STRUCTURE OF THE C3HC4 DOMAIN BY 1H-NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; A NEW STRUCTURAL CLASS OF ZINC-FINGER'''
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== Function ==
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[https://www.uniprot.org/uniprot/ICP0_EHV1B ICP0_EHV1B] Evades nuclear antiviral defenses triggered by dsDNA viruses. Acts during the initial stages of lytic infection and the reactivation of latent viral genome. Prevents the antiviral effect of nuclear bodies by degrading host PML and SP100.
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ch/1chc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1chc ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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.
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.
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==About this Structure==
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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<ref>PMID:8126734</ref>
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1CHC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Equid_herpesvirus_1 Equid herpesvirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CHC OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/8126734 8126734]
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</div>
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[[Category: Equid herpesvirus 1]]
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<div class="pdbe-citations 1chc" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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[[Category: Barlow, P N.]]
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<references/>
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[[Category: Everett, R D.]]
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__TOC__
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[[Category: Luisi, B.]]
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</StructureSection>
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[[Category: Viral protein]]
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[[Category: Equid alphaherpesvirus 1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:44:01 2008''
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[[Category: Large Structures]]
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[[Category: Barlow PN]]
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[[Category: Everett RD]]
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[[Category: Luisi B]]

Current revision

STRUCTURE OF THE C3HC4 DOMAIN BY 1H-NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; A NEW STRUCTURAL CLASS OF ZINC-FINGER

PDB ID 1chc

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