Transcription Termination Factor Rho

From Proteopedia

PDB ID 1pvo Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
E. coli transcription termination factor Rho complex wit ssRNA and ANPPNP, 1pvo
Ligands:
Gene:	RHO (Escherichia coli)
Related:	1pv4
Structural annotation: Resources: InterPro : Ipr011112, Ipr011129, Ipr002110, Ipr000194, Ipr004665, Ipr003593, Ipr011113 Pfam : PF07498, PF00006, PF07497 SCOP : d1pvoa2, d1pvoa3, d1pvoa1, d1pvob1, d1pvob2, d1pvoc3, d1pvoc2, d1pvoc1, d1pvod2, d1pvod1, d1pvod3, d1pvoe3, d1pvoe2, d1pvoe1, d1pvof1, d1pvof3, d1pvof2 UniProt : P0AG30
Functional annotation: Cellular component: proton-transporting two-sector ATPase complex membrane fraction Biological process: transcription termination transcription regulation of transcription, DNA-dependent ATP synthesis coupled proton transport Molecular function: protein binding hydrogen ion transporting ATP synthase activity, rotational mechanism hydrogen ion transporting ATPase activity, rotational mechanism nucleotide binding helicase activity transcription termination factor activity RNA binding ATP binding nucleoside-triphosphatase activity hydrolase activity nucleic acid binding
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

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]. Note that this model has only the middle 324 amino acids in each chain, lacking the first 52 and the last 57 amino acids in each chain^[2].

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 . In this scene, the foreground RNA is colored by element (C O N P). Also colored are Lys181, Lys283, Arg347, Arg353, and (in black) background RNA. See also Transcription and RNA Processing.

3D structures of helicase

Helicase

Additional Resources

For additional information, see: Transcription and RNA Processing

Notes

1. ↑ File Image:Rho1.pdb derived from 2ht1 by symmetry operations
2. ↑ Missing residues can be found by aligning the PDB file's SEQRES records with the sequence of the residues assigned atomic coordinates, as listed by the S2C Server