1I50

RNA POLYMERASE II CRYSTAL FORM II AT 2.8 A RESOLUTION

Summary for 1I50

• Entry DOI: 10.2210/pdb1i50/pdb
• Related: 1EN0 1I3Q
• Descriptor: DNA-DIRECTED RNA POLYMERASE II LARGEST SUBUNIT, DNA-DIRECTED RNA POLYMERASE II 7.7KD POLYPEPTIDE, ZINC ION, ... (13 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 P38902; Nucleus, nucleolus : P40422 P27999 P22139; Cytoplasm : P20435
• Total number of polymer chains: 10
• Total formula weight: 470204.19

Authors

Cramer, P.,Bushnell, D.A.,Kornberg, R.D. (deposition date: 2001-02-23, release date: 2001-04-23, Last modification date: 2024-02-07)

Primary citation

Cramer, P.,Bushnell, D.A.,Kornberg, R.D.
Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution.
Science, 292:1863-1876, 2001

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

Experimental method

X-RAY DIFFRACTION (2.8 Å)