1pvo: Difference between revisions

Line 1:

[[Image:1pvo.gif|left|200px]]<br /><applet load="1pvo" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1pvo.gif|left|200px]]<br /><applet load="1pvo" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1pvo, resolution 3.00Å" />

'''X-ray crystal structure of Rho transcription termination factor in complex with ssRNA substrate and ANPPNP'''<br />

==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.

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 [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].

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==

Line 13:

[[Category: Escherichia coli]]

[[Category: Single protein]]

[[Category: Berger, J.M.]]

[[Category: Berger, J M.]]

[[Category: Skordalakes, E.]]

[[Category: ANP]]

[[Category: rho-anppnp-ssrna complex]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 00:09:~~43 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:32:59 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1pvo.gif|left|200px]]<br /><applet load="1pvo" size="450" color="white" frame="true" align="right" spinBox="true"
+[[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;" />
 '''X-ray crystal structure of Rho transcription termination factor in complex with ssRNA substrate and ANPPNP'''<br />
 ==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.
+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==
-PVO 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].
+PVO 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==
@@ Line 13: / Line 13: @@
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Berger, J.M.]]
+[[Category: Berger, J M.]]
 [[Category: Skordalakes, E.]]
 [[Category: ANP]]
 [[Category: rho-anppnp-ssrna complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:09:43 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:32:59 2008''