6F44
RNA Polymerase III closed complex CC2.
Summary for 6F44
| Entry DOI | 10.2210/pdb6f44/pdb |
| Related | 6F40 6F41 6F42 |
| EMDB information | 4180 4181 4182 4183 4184 |
| Descriptor | DNA-directed RNA polymerase III subunit RPC1, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerases I and III subunit RPAC2, ... (23 entities in total) |
| Functional Keywords | transcription, rna polymerase iii, tfiiib, pre-initiation complex, brf1, bdp1, tbp, pol iii, enzyme |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Total number of polymer chains | 22 |
| Total formula weight | 906357.79 |
| Authors | Vorlaender, M.K.,Khatter, H.,Wetzel, R.,Hagen, W.J.H.,Mueller, C.W. (deposition date: 2017-11-29, release date: 2018-01-17, Last modification date: 2024-11-13) |
| Primary citation | Vorlander, M.K.,Khatter, H.,Wetzel, R.,Hagen, W.J.H.,Muller, C.W. Molecular mechanism of promoter opening by RNA polymerase III. Nature, 553:295-300, 2018 Cited by PubMed Abstract: RNA polymerase III (Pol III) and transcription factor IIIB (TFIIIB) assemble together on different promoter types to initiate the transcription of small, structured RNAs. Here we present structures of Pol III preinitiation complexes, comprising the 17-subunit Pol III and the heterotrimeric transcription factor TFIIIB, bound to a natural promoter in different functional states. Electron cryo-microscopy reconstructions, varying from 3.7 Å to 5.5 Å resolution, include two early intermediates in which the DNA duplex is closed, an open DNA complex, and an initially transcribing complex with RNA in the active site. Our structures reveal an extremely tight, multivalent interaction between TFIIIB and promoter DNA, and explain how TFIIIB recruits Pol III. Together, TFIIIB and Pol III subunit C37 activate the intrinsic transcription factor-like activity of the Pol III-specific heterotrimer to initiate the melting of double-stranded DNA, in a mechanism similar to that of the Pol II system. PubMed: 29345638DOI: 10.1038/nature25440 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.2 Å) |
Structure validation
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