2E2J
RNA polymerase II elongation complex in 5 mM Mg+2 with GMPCPP
Summary for 2E2J
Entry DOI | 10.2210/pdb2e2j/pdb |
Related | 1R9S 1R9T 1SFO 2E2H 2E2I 2NVQ 2NVS 2NVT 2NVX 2NVY 2NVZ |
Descriptor | 5'-R(P*AP*UP*CP*GP*AP*GP*AP*GP*G)-3', DNA-directed RNA polymerase II subunit 9, DNA-directed RNA polymerases I/II/III subunit 10, ... (16 entities in total) |
Functional Keywords | transcription, mrna, multiprotein complex, molecular machine, dna, transcription-dna-rna complex, transferase-dna-rna hybrid complex, transferase/dna-rna hybrid |
Biological source | Saccharomyces cerevisiae (baker's yeast) More |
Total number of polymer chains | 13 |
Total formula weight | 485841.81 |
Authors | Wang, D.,Bushnell, D.A.,Westover, K.D.,Kaplan, C.D.,Kornberg, R.D. (deposition date: 2006-11-14, release date: 2006-12-12, Last modification date: 2023-10-25) |
Primary citation | Wang, D.,Bushnell, D.A.,Westover, K.D.,Kaplan, C.D.,Kornberg, R.D. Structural basis of transcription: role of the trigger loop in substrate specificity and catalysis Cell(Cambridge,Mass.), 127:941-954, 2006 Cited by PubMed Abstract: New structures of RNA polymerase II (pol II) transcribing complexes reveal a likely key to transcription. The trigger loop swings beneath a correct nucleoside triphosphate (NTP) in the nucleotide addition site, closing off the active center and forming an extensive network of interactions with the NTP base, sugar, phosphates, and additional pol II residues. A histidine side chain in the trigger loop, precisely positioned by these interactions, may literally "trigger" phosphodiester bond formation. Recognition and catalysis are thus coupled, ensuring the fidelity of transcription. PubMed: 17129781DOI: 10.1016/j.cell.2006.11.023 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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