1TWH
RNA polymerase II complexed with 2'dATP
Summary for 1TWH
| Entry DOI | 10.2210/pdb1twh/pdb |
| Related | 1twa 1twc 1twf 1twg |
| Descriptor | DNA-directed RNA polymerase II largest subunit, DNA-directed RNA polymerases I, II, and III 7.7 kDa polypeptide, MANGANESE (II) ION, ... (14 entities in total) |
| Functional Keywords | transcription, mrna, multiprotein complex, molecular machine, zinc motifs |
| Biological source | Saccharomyces cerevisiae (baker's yeast) More |
| Cellular location | Nucleus: P04050 P08518 P16370 P20434 P20436 P27999 P38902 Nucleus, nucleolus: P40422 P22139 Cytoplasm: P20435 |
| Total number of polymer chains | 10 |
| Total formula weight | 470766.31 |
| Authors | Westover, K.D.,Bushnell, D.A.,Kornberg, R.D. (deposition date: 2004-06-30, release date: 2004-11-16, Last modification date: 2024-10-30) |
| Primary citation | Westover, K.D.,Bushnell, D.A.,Kornberg, R.D. Structural basis of transcription: nucleotide selection by rotation in the RNA polymerase II active center. Cell(Cambridge,Mass.), 119:481-489, 2004 Cited by PubMed Abstract: Binding of a ribonucleoside triphosphate to an RNA polymerase II transcribing complex, with base pairing to the template DNA, was revealed by X-ray crystallography. Binding of a mismatched nucleoside triphosphate was also detected, but in an adjacent site, inverted with respect to the correctly paired nucleotide. The results are consistent with a two-step mechanism of nucleotide selection, with initial binding to an entry (E) site beneath the active center in an inverted orientation, followed by rotation into the nucleotide addition (A) site for pairing with the template DNA. This mechanism is unrelated to that of single subunit RNA polymerases and so defines a new paradigm for the large, multisubunit enzymes. Additional findings from these studies include a third nucleotide binding site that may define the length of backtracked RNA; DNA double helix unwinding in advance of the polymerase active center; and extension of the diffraction limit of RNA polymerase II crystals to 2.3 A. PubMed: 15537538DOI: 10.1016/j.cell.2004.10.016 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.4 Å) |
Structure validation
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