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1pvo

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1pvo, resolution 3.00Å ()

Ligands:

Gene:

RHO (Escherichia coli)

Domains:

PP-binding, COG3320, adh_short, KR, Acyl_transf_1, PKS, rho, rho_factor, Rho_RNA_bind, Rho_N

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

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

X-ray crystal structure of Rho transcription termination factor in complex with ssRNA substrate and ANPPNP

Publication Abstract from PubMed

In bacteria, one of the major transcriptional termination mechanisms requires a RNA/DNA helicase known as the Rho factor. We have determined two structures of Rho complexed with nucleic acid recognition site mimics in both free and nucleotide bound states to 3.0 A resolution. Both structures show that Rho forms a hexameric ring in which two RNA binding sites--a primary one responsible for target mRNA recognition and a secondary one required for mRNA translocation and unwinding--point toward the center of the ring. Rather than forming a closed ring, the Rho hexamer is split open, resembling a "lock washer" in its global architecture. The distance between subunits at the opening is sufficiently wide (12 A) to accommodate single-stranded RNA. This open configuration most likely resembles a state poised to load onto mRNA and suggests how related ring-shaped enzymes may be breached to bind nucleic acids.

Structure of the Rho transcription terminator: mechanism of mRNA recognition and helicase loading., Skordalakes E, Berger JM, Cell. 2003 Jul 11;114(1):135-46. PMID:12859904

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1PVO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of the Rho transcription terminator: mechanism of mRNA recognition and helicase loading., Skordalakes E, Berger JM, Cell. 2003 Jul 11;114(1):135-46. PMID:12859904

Page seeded by OCA on Mon Jul 28 17:35:32 2008