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| - | ==STRUCTURE OF THE EPSTEIN-BARR VIRUS ZEBRA PROTEIN== | + | |
| - | <StructureSection load='2c9l' size='340' side='right' caption='[[2c9l]], [[Resolution|resolution]] 2.25Å' scene=''> | + | ==Structure of the Epstein-Barr virus ZEBRA protein== |
| | + | <StructureSection load='2c9l' size='340' side='right'caption='[[2c9l]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2c9l]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C9L FirstGlance]. <br> | + | <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><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zsd|1zsd]], [[2axf|2axf]], [[2axg|2axg]], [[2c9n|2c9n]]</td></tr> | + | </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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c9l RCSB], [http://www.ebi.ac.uk/pdbsum/2c9l PDBsum]</span></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> | + | </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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 2c9l" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human herpesvirus 4]] | + | [[Category: Human gammaherpesvirus 4]] |
| - | [[Category: Artero, J B.]] | + | [[Category: Large Structures]] |
| - | [[Category: Baudin, F.]] | + | [[Category: Artero JB]] |
| - | [[Category: Morand, P.]] | + | [[Category: Baudin F]] |
| - | [[Category: Moulin, M.]] | + | [[Category: Morand P]] |
| - | [[Category: Muller, C W.]] | + | [[Category: Moulin M]] |
| - | [[Category: Petosa, C.]] | + | [[Category: Muller CW]] |
| - | [[Category: Bzip protein]]
| + | [[Category: Petosa C]] |
| - | [[Category: Bzlf1]]
| + | |
| - | [[Category: Ebv]]
| + | |
| - | [[Category: Epstein-barr virus]]
| + | |
| - | [[Category: Lytic cycle activation]]
| + | |
| - | [[Category: Nuclear protein]]
| + | |
| - | [[Category: Transcription regulation]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| - | [[Category: Viral protein dna-binding]]
| + | |
| - | [[Category: Zebra]]
| + | |
| - | [[Category: Zta]]
| + | |
| Structural highlights
Function
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).[1] [2] [3] [4] [5]
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.
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[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Packham G, Economou A, Rooney CM, Rowe DT, Farrell PJ. Structure and function of the Epstein-Barr virus BZLF1 protein. J Virol. 1990 May;64(5):2110-6. PMID:2157874
- ↑ Kouzarides T, Packham G, Cook A, Farrell PJ. The BZLF1 protein of EBV has a coiled coil dimerisation domain without a heptad leucine repeat but with homology to the C/EBP leucine zipper. Oncogene. 1991 Feb;6(2):195-204. PMID:1847997
- ↑ Schepers A, Pich D, Hammerschmidt W. A transcription factor with homology to the AP-1 family links RNA transcription and DNA replication in the lytic cycle of Epstein-Barr virus. EMBO J. 1993 Oct;12(10):3921-9. PMID:8404860
- ↑ Wen W, Iwakiri D, Yamamoto K, Maruo S, Kanda T, Takada K. Epstein-Barr virus BZLF1 gene, a switch from latency to lytic infection, is expressed as an immediate-early gene after primary infection of B lymphocytes. J Virol. 2007 Jan;81(2):1037-42. Epub 2006 Nov 1. PMID:17079287 doi:10.1128/JVI.01416-06
- ↑ McDonald CM, Petosa C, Farrell PJ. Interaction of Epstein-Barr virus BZLF1 C-terminal tail structure and core zipper is required for DNA replication but not for promoter transactivation. J Virol. 2009 Apr;83(7):3397-401. doi: 10.1128/JVI.02500-08. Epub 2009 Jan 14. PMID:19144704 doi:10.1128/JVI.02500-08
- ↑ Petosa C, Morand P, Baudin F, Moulin M, Artero JB, Muller CW. Structural basis of lytic cycle activation by the Epstein-Barr virus ZEBRA protein. Mol Cell. 2006 Feb 17;21(4):565-72. PMID:16483937 doi:S1097-2765(06)00007-4
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