1hwq: Difference between revisions

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New page: left|200px<br /><applet load="1hwq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hwq" /> '''SOLUTION STRUCTURE OF THE VS RIBOZYME SUBSTR...
 
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[[Image:1hwq.gif|left|200px]]<br /><applet load="1hwq" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1hwq.gif|left|200px]]<br /><applet load="1hwq" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1hwq" />
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'''SOLUTION STRUCTURE OF THE VS RIBOZYME SUBSTRATE STEM-LOOP'''<br />
'''SOLUTION STRUCTURE OF THE VS RIBOZYME SUBSTRATE STEM-LOOP'''<br />


==Overview==
==Overview==
The VS ribozyme is a 154 nucleotide sequence found in certain natural, strains of Neurospora. The RNA can be divided into a substrate and a, catalytic domain. Here we present the solution structure of the substrate, RNA that is cleaved in a trans reaction by the catalytic domain in the, presence of Mg2+. The 30 nucleotide substrate RNA forms a compact helix, capped by a flexible loop. The cleavage site bulge contains three, non-canonical base-pairs, including an A+.C pair with a protonated, adenine. This adenine (A622) is a pH controlled conformational switch that, opens up the internal loop at higher pH. The possible significance of this, switch for substrate recognition and cleavage is discussed.
The VS ribozyme is a 154 nucleotide sequence found in certain natural strains of Neurospora. The RNA can be divided into a substrate and a catalytic domain. Here we present the solution structure of the substrate RNA that is cleaved in a trans reaction by the catalytic domain in the presence of Mg2+. The 30 nucleotide substrate RNA forms a compact helix capped by a flexible loop. The cleavage site bulge contains three non-canonical base-pairs, including an A+.C pair with a protonated adenine. This adenine (A622) is a pH controlled conformational switch that opens up the internal loop at higher pH. The possible significance of this switch for substrate recognition and cleavage is discussed.


==About this Structure==
==About this Structure==
1HWQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HWQ OCA].  
1HWQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HWQ OCA].  


==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Dieckmann, T.]]
[[Category: Dieckmann, T.]]
[[Category: Flinders, J.C.]]
[[Category: Flinders, J C.]]
[[Category: a+c base pair]]
[[Category: a+c base pair]]
[[Category: protonated adenine]]
[[Category: protonated adenine]]
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[[Category: vs ribozyme]]
[[Category: vs ribozyme]]


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Revision as of 14:05, 21 February 2008

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1hwq

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SOLUTION STRUCTURE OF THE VS RIBOZYME SUBSTRATE STEM-LOOP

OverviewOverview

The VS ribozyme is a 154 nucleotide sequence found in certain natural strains of Neurospora. The RNA can be divided into a substrate and a catalytic domain. Here we present the solution structure of the substrate RNA that is cleaved in a trans reaction by the catalytic domain in the presence of Mg2+. The 30 nucleotide substrate RNA forms a compact helix capped by a flexible loop. The cleavage site bulge contains three non-canonical base-pairs, including an A+.C pair with a protonated adenine. This adenine (A622) is a pH controlled conformational switch that opens up the internal loop at higher pH. The possible significance of this switch for substrate recognition and cleavage is discussed.

About this StructureAbout this Structure

1HWQ is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.

ReferenceReference

A pH controlled conformational switch in the cleavage site of the VS ribozyme substrate RNA., Flinders J, Dieckmann T, J Mol Biol. 2001 May 11;308(4):665-79. PMID:11350168

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