6HLQ
Yeast RNA polymerase I* elongation complex bound to nucleotide analog GMPCPP
Summary for 6HLQ
| Entry DOI | 10.2210/pdb6hlq/pdb |
| EMDB information | 0238 0239 |
| Descriptor | DNA-directed RNA polymerase I subunit RPA190, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerases I and III subunit RPAC2, ... (18 entities in total) |
| Functional Keywords | transcription, polymerase, nucleotide, elongation |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Total number of polymer chains | 15 |
| Total formula weight | 547427.68 |
| Authors | Tafur, L.,Sadian, Y.,Weis, F.,Muller, C.W. (deposition date: 2018-09-11, release date: 2019-04-03, Last modification date: 2024-05-15) |
| Primary citation | Tafur, L.,Sadian, Y.,Hanske, J.,Wetzel, R.,Weis, F.,Muller, C.W. The cryo-EM structure of a 12-subunit variant of RNA polymerase I reveals dissociation of the A49-A34.5 heterodimer and rearrangement of subunit A12.2. Elife, 8:-, 2019 Cited by PubMed Abstract: RNA polymerase (Pol) I is a 14-subunit enzyme that solely transcribes pre-ribosomal RNA. Cryo-electron microscopy (EM) structures of Pol I initiation and elongation complexes have given first insights into the molecular mechanisms of Pol I transcription. Here, we present cryo-EM structures of yeast Pol I elongation complexes (ECs) bound to the nucleotide analog GMPCPP at 3.2 to 3.4 Å resolution that provide additional insight into the functional interplay between the Pol I-specific transcription-like factors A49-A34.5 and A12.2. Strikingly, most of the nucleotide-bound ECs lack the A49-A34.5 heterodimer and adopt a Pol II-like conformation, in which the A12.2 C-terminal domain is bound in a previously unobserved position at the A135 surface. Our structural and biochemical data suggest a mechanism where reversible binding of the A49-A34.5 heterodimer could contribute to the regulation of Pol I transcription initiation and elongation. PubMed: 30913026DOI: 10.7554/eLife.43204 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.18 Å) |
Structure validation
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