1NT9
Complete 12-subunit RNA polymerase II
Summary for 1NT9
| Entry DOI | 10.2210/pdb1nt9/pdb |
| Related | 1G03 1I3Q 1I50 1I6H |
| Descriptor | DNA-DIRECTED RNA POLYMERASE II LARGEST SUBUNIT, DNA-directed RNA polymerases I, II, and III 8.3 kDa polypeptide, DNA-DIRECTED RNA POLYMERASE II 13.6 KD POLYPEPTIDE, ... (12 entities in total) |
| Functional Keywords | dna-dependent rna polymerase; cellular rna polymerase; multisubunit complex; transcription; gene expression; mrna; messenger rna synthesis, transcription, transferase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) More |
| Cellular location | Nucleus: P04050 P38902 P08518 P16370 P20433 P20434 P34087 P20436 P27999 Nucleus, nucleolus: P22139 P40422 Cytoplasm: P20435 |
| Total number of polymer chains | 12 |
| Total formula weight | 514158.22 |
| Authors | Armache, K.-J.,Kettenberger, H.,Cramer, P. (deposition date: 2003-01-29, release date: 2003-04-22, Last modification date: 2023-08-16) |
| Primary citation | Armache, K.-J.,Kettenberger, H.,Cramer, P. Architecture of initiation-competent 12-subunit RNA polymerase II Proc.Natl.Acad.Sci.USA, 100:6964-6968, 2003 Cited by PubMed Abstract: RNA polymerase (Pol) II consists of a 10-polypeptide catalytic core and the two-subunit Rpb4/7 complex that is required for transcription initiation. Previous structures of the Pol II core revealed a "clamp," which binds the DNA template strand via three "switch regions," and a flexible "linker" to the C-terminal repeat domain (CTD). Here we derived a model of the complete Pol II by fitting structures of the core and Rpb4/7 to a 4.2-A crystallographic electron density map. Rpb4/7 protrudes from the polymerase "upstream face," on which initiation factors assemble for promoter DNA loading. Rpb7 forms a wedge between the clamp and the linker, restricting the clamp to a closed position. The wedge allosterically prevents entry of the promoter DNA duplex into the active center cleft and induces in two switch regions a conformation poised for template-strand binding. Interaction of Rpb4/7 with the linker explains Rpb4-mediated recruitment of the CTD phosphatase to the CTD during Pol II recycling. The core-Rpb7 interaction and some functions of Rpb4/7 are apparently conserved in all eukaryotic and archaeal RNA polymerases but not in the bacterial enzyme. PubMed: 12746495DOI: 10.1073/pnas.1030608100 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.2 Å) |
Structure validation
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