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1BJA

ACTIVATION DOMAIN OF THE PHAGE T4 TRANSCRIPTION FACTOR MOTA

Summary for 1BJA
Entry DOI10.2210/pdb1bja/pdb
DescriptorTRANSCRIPTION REGULATORY PROTEIN MOTA, SULFATE ION (3 entities in total)
Functional Keywordsactivation domain, phage t4, middle mode transcription, alpha helical structure, transcription regulation
Biological sourceEnterobacteria phage T4
Total number of polymer chains2
Total formula weight20325.21
Authors
Finnin, M.S.,Cicero, M.P.,Davies, C.,Porter, S.J.,White, S.W.,Kreuzer, K.N. (deposition date: 1998-06-23, release date: 1998-11-04, Last modification date: 2024-02-07)
Primary citationFinnin, M.S.,Cicero, M.P.,Davies, C.,Porter, S.J.,White, S.W.,Kreuzer, K.N.
The activation domain of the MotA transcription factor from bacteriophage T4.
EMBO J., 16:1992-2003, 1997
Cited by
PubMed Abstract: 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.
PubMed: 9155025
DOI: 10.1093/emboj/16.8.1992
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.19 Å)
Structure validation

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