Summary information and primary citation
- PDB-id
-
1i6h;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- transcription-DNA-RNA hybrid
- Method
- X-ray (3.3 Å)
- Summary
- RNA polymerase ii elongation complex
- Reference
-
Gnatt AL, Cramer P, Fu J, Bushnell DA, Kornberg RD
(2001): "Structural
basis of transcription: an RNA polymerase II elongation
complex at 3.3 A resolution." Science,
292, 1876-1882. doi: 10.1126/science.1059495.
- Abstract
- The crystal structure of RNA polymerase II in the act
of transcription was determined at 3.3 A resolution. Duplex
DNA is seen entering the main cleft of the enzyme and
unwinding before the active site. Nine base pairs of
DNA-RNA hybrid extend from the active center at nearly
right angles to the entering DNA, with the 3' end of the
RNA in the nucleotide addition site. The 3' end is
positioned above a pore, through which nucleotides may
enter and through which RNA may be extruded during
back-tracking. The 5'-most residue of the RNA is close to
the point of entry to an exit groove. Changes in protein
structure between the transcribing complex and free enzyme
include closure of a clamp over the DNA and RNA and
ordering of a series of "switches" at the base of the clamp
to create a binding site complementary to the DNA-RNA
hybrid. Protein-nucleic acid contacts help explain DNA and
RNA strand separation, the specificity of RNA synthesis,
"abortive cycling" during transcription initiation, and RNA
and DNA translocation during transcription elongation.