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| | <StructureSection load='5gpy' size='340' side='right'caption='[[5gpy]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='5gpy' size='340' side='right'caption='[[5gpy]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5gpy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GPY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GPY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5gpy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GPY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GPY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GTF2E1, TF2E1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), GTF2E2, TF2E2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5gpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gpy OCA], [http://pdbe.org/5gpy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gpy RCSB], [http://www.ebi.ac.uk/pdbsum/5gpy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gpy ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5gpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gpy OCA], [https://pdbe.org/5gpy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gpy RCSB], [https://www.ebi.ac.uk/pdbsum/5gpy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gpy ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/T2EA_HUMAN T2EA_HUMAN]] Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase. [[http://www.uniprot.org/uniprot/T2EB_HUMAN T2EB_HUMAN]] Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase. | + | [https://www.uniprot.org/uniprot/T2EA_HUMAN T2EA_HUMAN] Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Transcription initiation factor|Transcription initiation factor]] | + | *[[Transcription initiation factors 3D structures|Transcription initiation factors 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kojima, R]] | + | [[Category: Kojima R]] |
| - | [[Category: Miwa, K]] | + | [[Category: Miwa K]] |
| - | [[Category: Mizuguchi, M]] | + | [[Category: Mizuguchi M]] |
| - | [[Category: Obita, T]] | + | [[Category: Obita T]] |
| - | [[Category: Ohkuma, Y]] | + | [[Category: Ohkuma Y]] |
| - | [[Category: Tamura, Y]] | + | [[Category: Tamura Y]] |
| - | [[Category: General transcription factor]]
| + | |
| - | [[Category: Rna polymerase ii]]
| + | |
| - | [[Category: Transcription]]
| + | |
| Structural highlights
Function
T2EA_HUMAN Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase.
Publication Abstract from PubMed
In eukaryotes, RNA polymerase II requires general transcription factors to initiate mRNA transcription. TFIIE subunits alpha and beta form a heterodimer and recruit TFIIH to complete the assembly of the pre-initiation complex. Here, we have determined the crystal structure of human TFIIE at atomic resolution. The N-terminal half of TFIIEalpha forms an extended winged helix (WH) domain with an additional helix, followed by a zinc-finger domain. TFIIEbeta contains the WH2 domain, followed by two coiled-coil helices intertwining with TFIIEalpha. We also showed that TFIIEalpha binds to TFIIEbeta with nanomolar affinity using isothermal titration calorimetry. In addition, mutations on the residues involved in the interactions resulted in severe growth defects in yeast. Lack of the C-terminal region of yeast TFIIEbeta causes a mild growth defect in vivo. These findings provide a structural basis for understanding the functional mechanisms of TFIIE in the context of pre-initiation complex formation and transcription initiation.
Crystal Structure of Human General Transcription Factor TFIIE at Atomic Resolution.,Miwa K, Kojima R, Obita T, Ohkuma Y, Tamura Y, Mizuguchi M J Mol Biol. 2016 Oct 23;428(21):4258-4266. doi: 10.1016/j.jmb.2016.09.008. Epub, 2016 Sep 15. PMID:27639436[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Miwa K, Kojima R, Obita T, Ohkuma Y, Tamura Y, Mizuguchi M. Crystal Structure of Human General Transcription Factor TFIIE at Atomic Resolution. J Mol Biol. 2016 Oct 23;428(21):4258-4266. doi: 10.1016/j.jmb.2016.09.008. Epub, 2016 Sep 15. PMID:27639436 doi:http://dx.doi.org/10.1016/j.jmb.2016.09.008
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