2C9L

Structure of the Epstein-Barr virus ZEBRA protein

Summary for 2C9L

• Entry DOI: 10.2210/pdb2c9l/pdb
• Related: 1ZSD 2AXF 2AXG 2C9N
• Descriptor: 5'-D(*AP*AP*GP*CP*AP*CP*TP*GP*AP*CP *TP*CP*AP*TP*GP*AP*AP*GP*T)-3', 5'-D(*AP*CP*TP*TP*CP*AP*CP*TP*GP*AP *GP*TP*CP*AP*GP*TP*GP*CP*T)-3', BZLF1 TRANS-ACTIVATOR PROTEIN, ... (4 entities in total)
• Functional Keywords: viral protein, epstein-barr virus, ebv, zebra, bzlf1, zta, z, lytic cycle activation, bzip protein, viral protein dna-binding, nuclear protein, transcription regulation
• Biological source: HUMAN HERPESVIRUS 4; More
• Cellular location: Host nucleus: 2C9L
• Total number of polymer chains: 4
• Total formula weight: 26171.87

Authors

Petosa, C.,Morand, P.,Baudin, F.,Moulin, M.,Artero, J.B.,Muller, C.W. (deposition date: 2005-12-13, release date: 2006-02-21, Last modification date: 2023-12-13)

Primary citation

Petosa, C.,Morand, P.,Baudin, F.,Moulin, M.,Artero, J.B.,Muller, C.W.
Structural Basis of Lytic Cycle Activation by the Epstein-Barr Virus Zebra Protein
Mol.Cell, 21:565-, 2006

PubMed Abstract: 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.

PubMed: 16483937
DOI: 10.1016/J.MOLCEL.2006.01.006

Experimental method

X-RAY DIFFRACTION (2.25 Å)