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-Structure paper
Title | Structure of TFIIK for phosphorylation of CTD of RNA polymerase II. |
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Journal, issue, pages | Sci Adv, Vol. 7, Issue 15, Year 2021 |
Publish date | Apr 7, 2021 |
Authors | Trevor van Eeuwen / Tao Li / Hee Jong Kim / Jose J Gorbea Colón / Mitchell I Parker / Roland L Dunbrack / Benjamin A Garcia / Kuang-Lei Tsai / Kenji Murakami / |
PubMed Abstract | During transcription initiation, the general transcription factor TFIIH marks RNA polymerase II by phosphorylating Ser5 of the carboxyl-terminal domain (CTD) of Rpb1, which is followed by extensive ...During transcription initiation, the general transcription factor TFIIH marks RNA polymerase II by phosphorylating Ser5 of the carboxyl-terminal domain (CTD) of Rpb1, which is followed by extensive modifications coupled to transcription elongation, mRNA processing, and histone dynamics. We have determined a 3.5-Å resolution cryo-electron microscopy (cryo-EM) structure of the TFIIH kinase module (TFIIK in yeast), which is composed of Kin28, Ccl1, and Tfb3, yeast homologs of CDK7, cyclin H, and MAT1, respectively. The carboxyl-terminal region of Tfb3 was lying at the edge of catalytic cleft of Kin28, where a conserved Tfb3 helix served to stabilize the activation loop in its active conformation. By combining the structure of TFIIK with the previous cryo-EM structure of the preinitiation complex, we extend the previously proposed model of the CTD path to the active site of TFIIK. |
External links | Sci Adv / PubMed:33827808 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.5 - 3.64 Å |
Structure data | EMDB-22191, PDB-6xi8: EMDB-23036, PDB-7kue: |
Chemicals | ChemComp-ADP: ChemComp-AF3: |
Source |
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Keywords | Transciption/Transferase / Polymerase CTD / TFIIH / Phosphorylation / Kinase / CDK / Cyclin / Transciption / Transciption-Transferase complex / TRANSCRIPTION/Transferase / TRANSCRIPTION-Transferase complex |