2c9l
From Proteopedia
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| - | [[Image:2c9l.gif|left|200px]]<br /><applet load="2c9l" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2c9l, resolution 2.25Å" /> | ||
| - | '''STRUCTURE OF THE EPSTEIN-BARR VIRUS ZEBRA PROTEIN'''<br /> | ||
| - | == | + | ==Structure of the Epstein-Barr virus ZEBRA protein== |
| + | <StructureSection load='2c9l' size='340' side='right'caption='[[2c9l]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2c9l]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_gammaherpesvirus_4 Human gammaherpesvirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C9L FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9l OCA], [https://pdbe.org/2c9l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c9l RCSB], [https://www.ebi.ac.uk/pdbsum/2c9l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c9l ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/BZLF1_EBVB9 BZLF1_EBVB9] Plays a key role in the switch from latent infection to lytic cycle producing new virions. Acts as a transcription factor, inducing early lytic cycle genes, and as a origin binding protein for genome replication. BZLF1 activates the promoter of another EBV gene (BSLF2+BMLF1).<ref>PMID:2157874</ref> <ref>PMID:1847997</ref> <ref>PMID:8404860</ref> <ref>PMID:17079287</ref> <ref>PMID:19144704</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Epstein-Barr virus (EBV) causes infectious mononucleosis and is linked to several human malignancies. EBV has a biphasic infection cycle consisting of a latent and a lytic, replicative phase. The switch from latent to lytic infection is triggered by the EBV immediate-early transcription factor ZEBRA (BZLF1, Zta, Z, EB1). We present the crystal structure of ZEBRA's DNA binding domain bound to an EBV lytic gene promoter element. ZEBRA exhibits a variant of the basic-region leucine zipper (bZIP) fold in which a C-terminal moiety stabilizes the coiled coil involved in dimer formation. The structure provides insights into ZEBRA's broad target site specificity, preferential activation of specific EBV promoters in their methylated state, ability to dimerize despite lacking a leucine zipper motif, and failure to heterodimerize with cellular bZIP proteins. The structure will allow for the design of new therapeutic agents that block activation of the EBV lytic cycle. | Epstein-Barr virus (EBV) causes infectious mononucleosis and is linked to several human malignancies. EBV has a biphasic infection cycle consisting of a latent and a lytic, replicative phase. The switch from latent to lytic infection is triggered by the EBV immediate-early transcription factor ZEBRA (BZLF1, Zta, Z, EB1). We present the crystal structure of ZEBRA's DNA binding domain bound to an EBV lytic gene promoter element. ZEBRA exhibits a variant of the basic-region leucine zipper (bZIP) fold in which a C-terminal moiety stabilizes the coiled coil involved in dimer formation. The structure provides insights into ZEBRA's broad target site specificity, preferential activation of specific EBV promoters in their methylated state, ability to dimerize despite lacking a leucine zipper motif, and failure to heterodimerize with cellular bZIP proteins. The structure will allow for the design of new therapeutic agents that block activation of the EBV lytic cycle. | ||
| - | + | Structural basis of lytic cycle activation by the Epstein-Barr virus ZEBRA protein.,Petosa C, Morand P, Baudin F, Moulin M, Artero JB, Muller CW Mol Cell. 2006 Feb 17;21(4):565-72. PMID:16483937<ref>PMID:16483937</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: Human | + | <div class="pdbe-citations 2c9l" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Artero | + | <references/> |
| - | [[Category: Baudin | + | __TOC__ |
| - | [[Category: Morand | + | </StructureSection> |
| - | [[Category: Moulin | + | [[Category: Human gammaherpesvirus 4]] |
| - | [[Category: Muller | + | [[Category: Large Structures]] |
| - | [[Category: Petosa | + | [[Category: Artero JB]] |
| - | + | [[Category: Baudin F]] | |
| - | + | [[Category: Morand P]] | |
| - | + | [[Category: Moulin M]] | |
| - | + | [[Category: Muller CW]] | |
| - | + | [[Category: Petosa C]] | |
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Current revision
Structure of the Epstein-Barr virus ZEBRA protein
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