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1pv4
From Proteopedia
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[[Image:1pv4.gif|left|200px]] | [[Image:1pv4.gif|left|200px]] | ||
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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''' | ||
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[[Category: Berger, J M.]] | [[Category: Berger, J M.]] | ||
[[Category: Skordalakes, E.]] | [[Category: Skordalakes, E.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:55:31 2008'' | |
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Revision as of 10:55, 30 April 2008
X-ray crystal structure of the Rho transcription termination factor in complex with single stranded DNA
Overview
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.
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 Wed Apr 30 13:55:31 2008
