Motion in Eukaryotic RNA Polymerase [rnapol]

[ jump to morphs ]

Classification Known Domain Motion, Hinge Mechanism [D-h-2]

Structures 1I50 Free complex 2I6H Elongation phase

Description Yeast RNA polymerase is a massive complex of twelve subunits (only ten in the initial crystal structures), two of which are longer than1000 residues. In the elongation phase, the N-terminal domain (approximately 340 residues) of the largest subunit has rotated in closer to the DNA strand.

References Gnatt AL, Cramer P, Fu J, Bushnell DA, Kornberg RD. Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 A resolution. Science. 2001 Jun 8;292(5523):1876-82. [Medline info for 11313499] Cramer P, Bushnell DA, Kornberg RD. Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution. Science. 2001 Jun 8;292(5523):1863-76. [Medline info for 11313498]

GO terms associated with structures Molecular function protein dimerization activity, DNA binding, transcription factor activity, DNA-directed RNA polymerase activity Cellular component nucleus, DNA-directed RNA polymerase II, core complex, RNA polymerase complex Biological process RNA elongation, transcription, DNA-dependent, regulation of transcription, DNA-dependent, transcription, regulation of transcription, transcription from RNA polymerase II promoter

Morphs

[ show all images ]

Best representative Morph Morph name Structure #1 Structure #2 Residues [ ] [ ]

---

Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu