1pv4: Difference between revisions
New page: left|200px<br /><applet load="1pv4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pv4, resolution 3.00Å" /> '''X-ray crystal struct... |
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[[Image:1pv4.gif|left|200px]]<br /><applet load="1pv4" size=" | [[Image:1pv4.gif|left|200px]]<br /><applet load="1pv4" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1pv4, resolution 3.00Å" /> | caption="1pv4, resolution 3.00Å" /> | ||
'''X-ray crystal structure of the Rho transcription termination factor in complex with single stranded DNA'''<br /> | '''X-ray crystal structure of the Rho transcription termination factor in complex with single stranded DNA'''<br /> | ||
==Overview== | ==Overview== | ||
In bacteria, one of the major transcriptional termination mechanisms | 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== | ==About this Structure== | ||
1PV4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | 1PV4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PV4 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Berger, J | [[Category: Berger, J M.]] | ||
[[Category: Skordalakes, E.]] | [[Category: Skordalakes, E.]] | ||
[[Category: protein-ssdna complex]] | [[Category: protein-ssdna complex]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:32:48 2008'' | ||
Revision as of 15:32, 21 February 2008
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X-ray crystal structure of the Rho transcription termination factor in complex with single stranded DNA
OverviewOverview
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 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
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