2hbl

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(New page: 200px<br /><applet load="2hbl" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hbl, resolution 2.300&Aring;" /> '''Structure of the ye...)
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[[Image:2hbl.gif|left|200px]]<br /><applet load="2hbl" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2hbl.gif|left|200px]]<br /><applet load="2hbl" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2hbl, resolution 2.300&Aring;" />
caption="2hbl, resolution 2.300&Aring;" />
'''Structure of the yeast nuclear exosome component, Rrp6p, reveals an interplay between the active site and the HRDC domain; Protein in complex with Mn, Zn, and AMP'''<br />
'''Structure of the yeast nuclear exosome component, Rrp6p, reveals an interplay between the active site and the HRDC domain; Protein in complex with Mn, Zn, and AMP'''<br />
==Overview==
==Overview==
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The multisubunit eukaryotic exosome is an essential RNA processing and, degradation machine. In its nuclear form, the exosome associates with the, auxiliary factor Rrp6p, which participates in both RNA processing and, degradation reactions. The crystal structure of Saccharomyces cerevisiae, Rrp6p displays a conserved RNase D core with a flanking HRDC (helicase and, RNase D C-terminal) domain in an unusual conformation shown to be, important for the processing function of the enzyme. Complexes with AMP, and UMP, the products of the RNA degradation process, reveal how the, protein specifically recognizes ribonucleotides and their bases. Finally, in vivo mutational studies show the importance of the domain contacts for, the processing function of Rrp6p and highlight fundamental differences, between the protein and its prokaryotic RNase D counterparts.
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The multisubunit eukaryotic exosome is an essential RNA processing and degradation machine. In its nuclear form, the exosome associates with the auxiliary factor Rrp6p, which participates in both RNA processing and degradation reactions. The crystal structure of Saccharomyces cerevisiae Rrp6p displays a conserved RNase D core with a flanking HRDC (helicase and RNase D C-terminal) domain in an unusual conformation shown to be important for the processing function of the enzyme. Complexes with AMP and UMP, the products of the RNA degradation process, reveal how the protein specifically recognizes ribonucleotides and their bases. Finally, in vivo mutational studies show the importance of the domain contacts for the processing function of Rrp6p and highlight fundamental differences between the protein and its prokaryotic RNase D counterparts.
==About this Structure==
==About this Structure==
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2HBL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with ZN, MN and AMP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HBL OCA].
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2HBL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=AMP:'>AMP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HBL OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Assenholt, J.]]
[[Category: Assenholt, J.]]
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[[Category: Brodersen, D.E.]]
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[[Category: Brodersen, D E.]]
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[[Category: Jensen, T.H.]]
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[[Category: Jensen, T H.]]
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[[Category: Jonstrup, A.T.]]
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[[Category: Jonstrup, A T.]]
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[[Category: Midtgaard, S.F.]]
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[[Category: Midtgaard, S F.]]
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[[Category: Van, L.B.]]
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[[Category: Van, L B.]]
[[Category: AMP]]
[[Category: AMP]]
[[Category: MN]]
[[Category: MN]]
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[[Category: rna surveillance]]
[[Category: rna surveillance]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:39:40 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:40:11 2008''

Revision as of 15:40, 21 February 2008


2hbl, resolution 2.300Å

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Structure of the yeast nuclear exosome component, Rrp6p, reveals an interplay between the active site and the HRDC domain; Protein in complex with Mn, Zn, and AMP

Overview

The multisubunit eukaryotic exosome is an essential RNA processing and degradation machine. In its nuclear form, the exosome associates with the auxiliary factor Rrp6p, which participates in both RNA processing and degradation reactions. The crystal structure of Saccharomyces cerevisiae Rrp6p displays a conserved RNase D core with a flanking HRDC (helicase and RNase D C-terminal) domain in an unusual conformation shown to be important for the processing function of the enzyme. Complexes with AMP and UMP, the products of the RNA degradation process, reveal how the protein specifically recognizes ribonucleotides and their bases. Finally, in vivo mutational studies show the importance of the domain contacts for the processing function of Rrp6p and highlight fundamental differences between the protein and its prokaryotic RNase D counterparts.

About this Structure

2HBL is a Single protein structure of sequence from Saccharomyces cerevisiae with , and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the nuclear exosome component Rrp6p reveals an interplay between the active site and the HRDC domain., Midtgaard SF, Assenholt J, Jonstrup AT, Van LB, Jensen TH, Brodersen DE, Proc Natl Acad Sci U S A. 2006 Aug 8;103(32):11898-903. Epub 2006 Aug 1. PMID:16882719

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