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1bja

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==ACTIVATION DOMAIN OF THE PHAGE T4 TRANSCRIPTION FACTOR MOTA==
==ACTIVATION DOMAIN OF THE PHAGE T4 TRANSCRIPTION FACTOR MOTA==
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<StructureSection load='1bja' size='340' side='right' caption='[[1bja]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
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<StructureSection load='1bja' size='340' side='right'caption='[[1bja]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1bja]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BJA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BJA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1bja]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BJA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BJA FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.19&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MOTA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 Enterobacteria phage T4])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bja OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bja RCSB], [http://www.ebi.ac.uk/pdbsum/1bja PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bja OCA], [https://pdbe.org/1bja PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bja RCSB], [https://www.ebi.ac.uk/pdbsum/1bja PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bja ProSAT]</span></td></tr>
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<table>
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</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/MOTA_BPT4 MOTA_BPT4] Required for the transcriptional activation of middle promoters. Middle promoters are characterized by the presence of the conserved sequence [AT]3TGCTTNA (MotA box). MotA binds directly to MotA boxes.
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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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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<ref>PMID:9155025</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Enterobacteria phage t4]]
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[[Category: Escherichia virus T4]]
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[[Category: Cicero, M P.]]
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[[Category: Large Structures]]
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[[Category: Davies, C.]]
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[[Category: Cicero MP]]
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[[Category: Finnin, M S.]]
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[[Category: Davies C]]
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[[Category: Kreuzer, K N.]]
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[[Category: Finnin MS]]
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[[Category: Porter, S J.]]
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[[Category: Kreuzer KN]]
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[[Category: White, S W.]]
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[[Category: Porter SJ]]
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[[Category: Activation domain]]
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[[Category: White SW]]
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[[Category: Alpha helical structure]]
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[[Category: Middle mode transcription]]
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[[Category: Phage t4]]
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[[Category: Transcription regulation]]
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Current revision

ACTIVATION DOMAIN OF THE PHAGE T4 TRANSCRIPTION FACTOR MOTA

PDB ID 1bja

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