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1I3Q

RNA POLYMERASE II CRYSTAL FORM I AT 3.1 A RESOLUTION

Replaces:  1EN0
Summary for 1I3Q
Entry DOI10.2210/pdb1i3q/pdb
Related1EN0
DescriptorDNA-DIRECTED RNA POLYMERASE II LARGEST SUBUNIT, DNA-DIRECTED RNA POLYMERASE II 7.7KD POLYPEPTIDE, ZINC ION, ... (12 entities in total)
Functional Keywordstranscription, mrna, multiprotein complex, molecular machine, zinc motifs
Biological sourceSaccharomyces cerevisiae (baker's yeast)
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Cellular locationNucleus: P04050 P08518 P16370 P20434 P20436 P27999 P38902
Nucleus, nucleolus: P40422 P22139
Cytoplasm: P20435
Total number of polymer chains10
Total formula weight470173.55
Authors
Cramer, P.,Bushnell, D.A.,Kornberg, R.D. (deposition date: 2001-02-15, release date: 2001-04-25, Last modification date: 2024-02-07)
Primary citationCramer, P.,Bushnell, D.A.,Kornberg, R.D.
Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution.
Science, 292:1863-1876, 2001
Cited by
PubMed Abstract: Structures of a 10-subunit yeast RNA polymerase II have been derived from two crystal forms at 2.8 and 3.1 angstrom resolution. Comparison of the structures reveals a division of the polymerase into four mobile modules, including a clamp, shown previously to swing over the active center. In the 2.8 angstrom structure, the clamp is in an open state, allowing entry of straight promoter DNA for the initiation of transcription. Three loops extending from the clamp may play roles in RNA unwinding and DNA rewinding during transcription. A 2.8 angstrom difference Fourier map reveals two metal ions at the active site, one persistently bound and the other possibly exchangeable during RNA synthesis. The results also provide evidence for RNA exit in the vicinity of the carboxyl-terminal repeat domain, coupling synthesis to RNA processing by enzymes bound to this domain.
PubMed: 11313498
DOI: 10.1126/science.1059493
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.1 Å)
Structure validation

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