1bja
From Proteopedia
(New page: 200px<br /><applet load="1bja" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bja, resolution 2.19Å" /> '''ACTIVATION DOMAIN OF...) |
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| - | [[Image:1bja.jpg|left|200px]]<br /><applet load="1bja" size=" | + | [[Image:1bja.jpg|left|200px]]<br /><applet load="1bja" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bja, resolution 2.19Å" /> | caption="1bja, resolution 2.19Å" /> | ||
'''ACTIVATION DOMAIN OF THE PHAGE T4 TRANSCRIPTION FACTOR MOTA'''<br /> | '''ACTIVATION DOMAIN OF THE PHAGE T4 TRANSCRIPTION FACTOR MOTA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Bacteriophage T4 encodes a transcription factor, MotA, that binds to the | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1BJA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1BJA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BJA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacteriophage t4]] | [[Category: Bacteriophage t4]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cicero, M | + | [[Category: Cicero, M P.]] |
[[Category: Davies, C.]] | [[Category: Davies, C.]] | ||
| - | [[Category: Finnin, M | + | [[Category: Finnin, M S.]] |
| - | [[Category: Kreuzer, K | + | [[Category: Kreuzer, K N.]] |
| - | [[Category: Porter, S | + | [[Category: Porter, S J.]] |
| - | [[Category: White, S | + | [[Category: White, S W.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: activation domain]] | [[Category: activation domain]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:55:53 2008'' |
Revision as of 09:55, 21 February 2008
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ACTIVATION DOMAIN OF THE PHAGE T4 TRANSCRIPTION FACTOR MOTA
Overview
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.
About this Structure
1BJA is a Single protein structure of sequence from Bacteriophage t4 with as ligand. 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
Page seeded by OCA on Thu Feb 21 11:55:53 2008
