Motion in Eukaryotic RNA Polymerase [rnapol]

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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 functionDNA binding, transcription factor activity, DNA-directed RNA polymerase activity, protein dimerization activity
Cellular componentDNA-directed RNA polymerase II, core complex, RNA polymerase complex, nucleus
Biological processregulation of transcription, DNA-dependent, transcription, regulation of transcription, transcription from RNA polymerase II promoter, RNA elongation, transcription, DNA-dependent

Morphs

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Best representative
Morph Morph name Structure #1 Structure #2 Residues
RNA Polymerase II 1i50 [ ] 1i6h [ ] 3500

User-submitted morphs
Morph Morph name Structure #1 Structure #2 Residues
961343-20634 RNA polymerase II 2n upload [ B ] upload [ B ] 539
961390-20655 RNA polymerase II 2n upload [ B ] upload [ B ] 539
954399-17898 RNA polymerase II la upload [ A ] upload [ A ] 690
956754-18587 RNA polymerase II la upload [ A ] upload [ A ] 691


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