1bja

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{{STRUCTURE_1bja| PDB=1bja | SCENE= }}
{{STRUCTURE_1bja| PDB=1bja | SCENE= }}
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'''ACTIVATION DOMAIN OF THE PHAGE T4 TRANSCRIPTION FACTOR MOTA'''
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===ACTIVATION DOMAIN OF THE PHAGE T4 TRANSCRIPTION FACTOR MOTA===
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==Overview==
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Bacteriophage T4 encodes a transcription factor, MotA, that binds to the -30 region of middle-mode promoters and activates transcription by host RNA polymerase. We have solved the structure of the MotA activation domain to 2.2 A by X-ray crystallography, and have also determined its secondary structure by NMR. An area on the surface of the protein has a distinctive patch that is populated with acidic and hydrophobic residues. Mutations within this patch cause a defective T4 growth phenotype, arguing that the patch is important for MotA function. One of the mutant MotA activation domains was purified and analyzed by NMR, and the spectra clearly show that the domain is properly folded. The mutant full-length protein appears to bind DNA normally but is deficient in transcriptional activation. We conclude that the acidic/hydrophobic surface patch is specifically involved in transcriptional activation, which is reminiscent of eukaryotic acidic activation domains.
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{{ABSTRACT_PUBMED_9155025}}
==About this Structure==
==About this Structure==
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[[Category: Phage t4]]
[[Category: Phage t4]]
[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
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Revision as of 16:15, 30 June 2008

Template:STRUCTURE 1bja

ACTIVATION DOMAIN OF THE PHAGE T4 TRANSCRIPTION FACTOR MOTA

Template:ABSTRACT PUBMED 9155025

About this Structure

1BJA is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

Reference

The activation domain of the MotA transcription factor from bacteriophage T4., Finnin MS, Cicero MP, Davies C, Porter SJ, White SW, Kreuzer KN, EMBO J. 1997 Apr 15;16(8):1992-2003. PMID:9155025

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