1pv4: Difference between revisions

Revision as of 04:40, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1pv4.png

Template:STRUCTURE 1pv4

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

Template:ABSTRACT PUBMED 12859904

About this StructureAbout this Structure

1PV4 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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

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OCA

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-'''X-ray crystal structure of the Rho transcription termination factor in complex with single stranded DNA'''
+===X-ray crystal structure of the Rho transcription termination factor in complex with single stranded DNA===
-==Overview==
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-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.
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 ==About this Structure==
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 [[Category: Skordalakes, E.]]
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