6GME
Structure of H. sapiens SPT6 tandem SH2 domain
Summary for 6GME
| Entry DOI | 10.2210/pdb6gme/pdb |
| Descriptor | SPT6 tandem SH2 domain,Transcription elongation factor SPT6 (2 entities in total) |
| Functional Keywords | sh2 domain, pol ii interaction, kinase target, transcription factor, transcription |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 2 |
| Total formula weight | 45792.53 |
| Authors | Vos, S.M.,Farnung, L.,Cramer, P. (deposition date: 2018-05-25, release date: 2018-08-22, Last modification date: 2024-01-17) |
| Primary citation | Vos, S.M.,Farnung, L.,Boehning, M.,Wigge, C.,Linden, A.,Urlaub, H.,Cramer, P. Structure of activated transcription complex Pol II-DSIF-PAF-SPT6. Nature, 560:607-612, 2018 Cited by PubMed Abstract: Gene regulation involves activation of RNA polymerase II (Pol II) that is paused and bound by the protein complexes DRB sensitivity-inducing factor (DSIF) and negative elongation factor (NELF). Here we show that formation of an activated Pol II elongation complex in vitro requires the kinase function of the positive transcription elongation factor b (P-TEFb) and the elongation factors PAF1 complex (PAF) and SPT6. The cryo-EM structure of an activated elongation complex of Sus scrofa Pol II and Homo sapiens DSIF, PAF and SPT6 was determined at 3.1 Å resolution and compared to the structure of the paused elongation complex formed by Pol II, DSIF and NELF. PAF displaces NELF from the Pol II funnel for pause release. P-TEFb phosphorylates the Pol II linker to the C-terminal domain. SPT6 binds to the phosphorylated C-terminal-domain linker and opens the RNA clamp formed by DSIF. These results provide the molecular basis for Pol II pause release and elongation activation. PubMed: 30135578DOI: 10.1038/s41586-018-0440-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.802 Å) |
Structure validation
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