3NFI
Crystal structure of tandem winged helix domain of RNA polymerase I subunit A49
Summary for 3NFI
Entry DOI | 10.2210/pdb3nfi/pdb |
Related | 3NFF 3NFG 3NFH |
Descriptor | DNA-directed RNA polymerase I subunit RPA49, 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL (3 entities in total) |
Functional Keywords | winged helix, transcription, rna polymerase, dna binding, dna binding protein |
Biological source | Saccharomyces cerevisiae (yeast) |
Cellular location | Nucleus, nucleolus : Q01080 |
Total number of polymer chains | 5 |
Total formula weight | 136063.01 |
Authors | Geiger, S.R.,Lorenzen, K.,Schreieck, A.,Hanecker, P.,Kostrewa, D.,Heck, A.J.R.,Cramer, P. (deposition date: 2010-06-10, release date: 2010-09-08, Last modification date: 2024-11-06) |
Primary citation | Geiger, S.R.,Lorenzen, K.,Schreieck, A.,Hanecker, P.,Kostrewa, D.,Heck, A.J.,Cramer, P. RNA Polymerase I Contains a TFIIF-Related DNA-Binding Subcomplex. Mol.Cell, 39:583-594, 2010 Cited by PubMed Abstract: The eukaryotic RNA polymerases Pol I, II, and III use different promoters to transcribe different classes of genes. Promoter usage relies on initiation factors, including TFIIF and TFIIE, in the case of Pol II. Here, we show that the Pol I-specific subunits A49 and A34.5 form a subcomplex that binds DNA and is related to TFIIF and TFIIE. The N-terminal regions of A49 and A34.5 form a dimerization module that stimulates polymerase-intrinsic RNA cleavage and has a fold that resembles the TFIIF core. The C-terminal region of A49 forms a "tandem winged helix" (tWH) domain that binds DNA with a preference for the upstream promoter nontemplate strand and is predicted in TFIIE. Similar domains are predicted in Pol III-specific subunits. Thus, Pol I/III subunits that have no counterparts in Pol II are evolutionarily related to Pol II initiation factors and may have evolved to mediate promoter specificity and transcription processivity. PubMed: 20797630DOI: 10.1016/j.molcel.2010.07.028 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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