1pvo

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(New page: 200px<br /><applet load="1pvo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pvo, resolution 3.00&Aring;" /> '''X-ray crystal struct...)
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[[Image:1pvo.gif|left|200px]]<br /><applet load="1pvo" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1pvo.gif|left|200px]]<br /><applet load="1pvo" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1pvo, resolution 3.00&Aring;" />
caption="1pvo, resolution 3.00&Aring;" />
'''X-ray crystal structure of Rho transcription termination factor in complex with ssRNA substrate and ANPPNP'''<br />
'''X-ray crystal structure of Rho transcription termination factor in complex with ssRNA substrate and ANPPNP'''<br />
==Overview==
==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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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==
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1PVO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ANP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PVO OCA].
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1PVO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ANP:'>ANP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PVO OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Berger, J.M.]]
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[[Category: Berger, J M.]]
[[Category: Skordalakes, E.]]
[[Category: Skordalakes, E.]]
[[Category: ANP]]
[[Category: ANP]]
[[Category: rho-anppnp-ssrna complex]]
[[Category: rho-anppnp-ssrna complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:09:43 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:32:59 2008''

Revision as of 12:33, 21 February 2008


1pvo, resolution 3.00Å

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

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

1PVO is a Single protein structure of sequence from Escherichia coli with as ligand. 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

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