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Instruments / Technical Area	Publication Details	Published	Actions
B21-High Throughput SAXS I02-Macromolecular Crystallography I04-Macromolecular Crystallography	The herpes viral transcription factor ICP4 forms a novel DNA recognition complex Richard B. Tunnicliffe , Michael P. Lockhart-Cairns , Colin Levy , A. Paul Mould , Thomas A. Jowitt , Hilary Sito , Clair Baldock , Rozanne M. Sandri-Goldin , Alexander P. Golovanov Nucleic Acids Research DOI: 10.1093/nar/gkx419 Diamond Proposal Number(s): [12788, 8997, 11534] Open Access Show Abstract ▼ Abstract: The transcription factor ICP4 from herpes simplex virus has a central role in regulating the gene expression cascade which controls viral infection. Here we present the crystal structure of the functionally essential ICP4 DNA binding domain in complex with a segment from its own promoter, revealing a novel homo-dimeric fold. We also studied the complex in solution by small angle X-Ray scattering, nuclear magnetic resonance and surface-plasmon resonance which indicated that, in addition to the globular domain, a flanking intrinsically disordered region also recognizes DNA. Together the data provides a rationale for the bi-partite nature of the ICP4 DNA recognition consensus sequence as the globular and disordered regions bind synergistically to adjacent DNA motifs. Therefore in common with its eukaryotic host, the viral transcription factor ICP4 utilizes disordered regions to enhance the affinity and tune the specificity of DNA interactions in tandem with a globular domain.	May 2017

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B21-High Throughput SAXS
I02-Macromolecular Crystallography
I04-Macromolecular Crystallography

The herpes viral transcription factor ICP4 forms a novel DNA recognition complex

Richard B. Tunnicliffe , Michael P. Lockhart-Cairns , Colin Levy , A. Paul Mould , Thomas A. Jowitt , Hilary Sito , Clair Baldock , Rozanne M. Sandri-Goldin , Alexander P. Golovanov

Nucleic Acids Research

DOI: 10.1093/nar/gkx419

Diamond Proposal Number(s): [12788, 8997, 11534]