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Transcription Termination Factor Rho
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'''Transcription termination factor Rho''' is a ring-shaped RNA-DNA '''helicase''' that induces release of transcription complexes at specific loci of bacterial genomes. Several structures of Rho in various liganded states haven been solved by X-ray crystallography by the J. M. Berger lab (Berkeley): [[1a8v]], [[1pv4]], [[1pvo]], [[1xpr]], [[1xpu]], [[2a8v]], and [[2ht1]]. | '''Transcription termination factor Rho''' is a ring-shaped RNA-DNA '''helicase''' that induces release of transcription complexes at specific loci of bacterial genomes. Several structures of Rho in various liganded states haven been solved by X-ray crystallography by the J. M. Berger lab (Berkeley): [[1a8v]], [[1pv4]], [[1pvo]], [[1xpr]], [[1xpu]], [[2a8v]], and [[2ht1]]. | ||
| - | The [[Asymmetric Unit|asymmetric unit]] solved as [[2ht1]] contains only two chains, so it represents only one third of the [[Biological Unit|biological unit]], which is a homo-hexamer. The scene here shows this <scene name='Transcription_Termination_Factor_Rho/Rho1_pdb_hexamer_overview/1'> | + | The [[Asymmetric Unit|asymmetric unit]] solved as [[2ht1]] contains only two chains, so it represents only one third of the [[Biological Unit|biological unit]], which is a homo-hexamer. The scene here shows this homo-hexamer in a closed state (<scene name='Transcription_Termination_Factor_Rho/Rho1_pdb_hexamer_overview/1'>restore initial scene</scene>)<ref>File [[Image:Rho1.pdb]] derived from [[2ht1]] by symmetry operations</ref>. In this model (<scene name='Transcription_Termination_Factor_Rho/Rho1_pdb_hexamer_overview/2'>show composition</scene>), the {{Template:ColorKey Composition Protein}} hexamer is bound to {{Template:ColorKey Composition RNA}}, and some incidental "{{Template:ColorKey Composition Solvent}}" (sulfate ions). |
Here is one representation showing the same Rho hexamer in a closed state and with <scene name='Transcription_Termination_Factor_Rho/Rho_closed_1/3'>RNA fragments occupying both its primary and secondary binding sites</scene>. | Here is one representation showing the same Rho hexamer in a closed state and with <scene name='Transcription_Termination_Factor_Rho/Rho_closed_1/3'>RNA fragments occupying both its primary and secondary binding sites</scene>. | ||
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| + | ==Notes== | ||
| + | <references /> | ||
Revision as of 21:12, 21 November 2008
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Transcription termination factor Rho is a ring-shaped RNA-DNA helicase that induces release of transcription complexes at specific loci of bacterial genomes. Several structures of Rho in various liganded states haven been solved by X-ray crystallography by the J. M. Berger lab (Berkeley): 1a8v, 1pv4, 1pvo, 1xpr, 1xpu, 2a8v, and 2ht1.
The asymmetric unit solved as 2ht1 contains only two chains, so it represents only one third of the biological unit, which is a homo-hexamer. The scene here shows this homo-hexamer in a closed state ()[1]. In this model (), the Protein hexamer is bound to RNA, and some incidental "Solvent" (sulfate ions).
Here is one representation showing the same Rho hexamer in a closed state and with .
Notes
- ↑ File Image:Rho1.pdb derived from 2ht1 by symmetry operations
