2c9n: Difference between revisions

Latest revision as of 10:25, 6 September 2023

Structure of the Epstein-Barr virus ZEBRA protein at approximately 3. 5 Angstrom resolution

Structural highlights

2c9n is a 4 chain structure with sequence from Human gammaherpesvirus 4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.3Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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

[2] 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

[3] 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

[4] 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

[5] 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

[6] 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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[2]

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[4]

[5]

[6]

@@ Line 3: / Line 3: @@
 <StructureSection load='2c9n' size='340' side='right'caption='[[2c9n]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2c9n]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ebvg Ebvg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C9N FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2c9n]] 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=2C9N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C9N FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1zsd|1zsd]], [[2axf|2axf]], [[2axg|2axg]], [[2c9l|2c9l]]</div></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]] 3.3&#8491;</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=2c9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9n OCA], [https://pdbe.org/2c9n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c9n RCSB], [https://www.ebi.ac.uk/pdbsum/2c9n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c9n 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 ==
@@ Line 20: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Ebvg]]
+[[Category: Human gammaherpesvirus 4]]
 [[Category: Large Structures]]
-[[Category: Artero, J B]]
+[[Category: Artero JB]]
-[[Category: Baudin, F]]
+[[Category: Baudin F]]
-[[Category: Morand, P]]
+[[Category: Morand P]]
-[[Category: Moulin, M]]
+[[Category: Moulin M]]
-[[Category: Muller, C W]]
+[[Category: Muller CW]]
-[[Category: Petosa, C]]
+[[Category: Petosa C]]
-[[Category: Bzip protein]]
-[[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]]

2c9n: Difference between revisions

Latest revision as of 10:25, 6 September 2023

Structure of the Epstein-Barr virus ZEBRA protein at approximately 3. 5 Angstrom resolution

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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