5gpy: Difference between revisions
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==Crystal structure of the human TFIIE complex== | |||
<StructureSection load='5gpy' size='340' side='right' caption='[[5gpy]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5gpy]] is a 2 chain structure. 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> | |||
</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> | |||
<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> | |||
</table> | |||
== 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. | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:27639436</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5gpy" style="background-color:#fffaf0;"></div> | |||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[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: Tamura, Y]] | |||
[[Category: General transcription factor]] | |||
[[Category: Rna polymerase ii]] | |||
[[Category: Transcription]] | |||
Revision as of 21:17, 2 November 2016
Crystal structure of the human TFIIE complexCrystal structure of the human TFIIE complex
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. [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. Publication Abstract from PubMedIn 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. References
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