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2E2J

RNA polymerase II elongation complex in 5 mM Mg+2 with GMPCPP

Summary for 2E2J
Entry DOI10.2210/pdb2e2j/pdb
Related1R9S 1R9T 1SFO 2E2H 2E2I 2NVQ 2NVS 2NVT 2NVX 2NVY 2NVZ
Descriptor5'-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 Keywordstranscription, mrna, multiprotein complex, molecular machine, dna, transcription-dna-rna complex, transferase-dna-rna hybrid complex, transferase/dna-rna hybrid
Biological sourceSaccharomyces cerevisiae (baker's yeast)
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Total number of polymer chains13
Total formula weight485841.81
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 citationWang, 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: 17129781
DOI: 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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