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1pv4

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1pv4, resolution 3.00Å ()

Non-Standard Residues:

Gene:

RHO (Escherichia coli)

Domains:

Peptidase_M14, rho, rho_factor, Rho_RNA_bind, Rho_N

Related:

1pvo

Structural annotation:
Resources:	CATH : 1Pv4A02, 1Pv4A01 InterPro : Ipr011129, Ipr002110, Ipr004665, Ipr011113, Ipr003593, Ipr000194, Ipr011112 Pfam : PF00006, PF07497, PF07498 SCOP : d1pv4a3, d1pv4a1, d1pv4a2, d1pv4b2, d1pv4b1, d1pv4c3, d1pv4c2, d1pv4c1, d1pv4d3, d1pv4d2, d1pv4d1, d1pv4e2, d1pv4e1, d1pv4e3, d1pv4f3, d1pv4f1, d1pv4f2 UniProt : P0AG30

Functional annotation:
Cellular component:	proton-transporting two-sector ATPase complex membrane fraction
Biological process:	regulation of transcription, DNA-dependent ATP synthesis coupled proton transport transcription transcription termination
Molecular function:	nucleoside-triphosphatase activity nucleic acid binding helicase activity hydrogen ion transporting ATP synthase activity, rotational mechanism protein binding nucleotide binding ATP binding RNA binding hydrogen ion transporting ATPase activity, rotational mechanism hydrolase activity transcription termination factor activity

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

X-ray crystal structure of the Rho transcription termination factor in complex with single stranded DNA

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

1PV4 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 Tue Jul 29 04:40:16 2008