2nn6: Difference between revisions

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==Overview==
==Overview==
The RNA exosome is a multisubunit 3' to 5' exoribonuclease complex that, participates in degradation and processing of cellular RNA. To determine, the activities and structure of the eukaryotic exosome, we report the, reconstitution of 9-subunit exosomes from yeast and human and, reconstitution of 10- and 11-subunit exosomes from yeast. Comparative, biochemical analysis between purified subunits and reconstituted exosomes, using AU-rich, polyadenylated (poly[A]), generic, and structured RNA, substrates reveals processive phosphorolytic activities for human, Rrp41/Rrp45 and the 9-subunit human exosome, processive hydrolytic, activities for yeast Rrp44 and the yeast 10-subunit exosome, distributive, hydrolytic activities for Rrp6, and processive and distributive hydrolytic, activities for the yeast 11-subunit exosome. To elucidate the architecture, of a eukaryotic exosome, its conserved surfaces, and the structural basis, for RNA decay, we report the X-ray structure determination for the 286 kDa, nine-subunit human exosome at 3.35 A.
The RNA exosome is a multisubunit 3' to 5' exoribonuclease complex that participates in degradation and processing of cellular RNA. To determine the activities and structure of the eukaryotic exosome, we report the reconstitution of 9-subunit exosomes from yeast and human and reconstitution of 10- and 11-subunit exosomes from yeast. Comparative biochemical analysis between purified subunits and reconstituted exosomes using AU-rich, polyadenylated (poly[A]), generic, and structured RNA substrates reveals processive phosphorolytic activities for human Rrp41/Rrp45 and the 9-subunit human exosome, processive hydrolytic activities for yeast Rrp44 and the yeast 10-subunit exosome, distributive hydrolytic activities for Rrp6, and processive and distributive hydrolytic activities for the yeast 11-subunit exosome. To elucidate the architecture of a eukaryotic exosome, its conserved surfaces, and the structural basis for RNA decay, we report the X-ray structure determination for the 286 kDa nine-subunit human exosome at 3.35 A.


==About this Structure==
==About this Structure==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Lima, C.D.]]
[[Category: Lima, C D.]]
[[Category: exoribonuclease]]
[[Category: exoribonuclease]]
[[Category: exosome]]
[[Category: exosome]]
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[[Category: rna]]
[[Category: rna]]


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Revision as of 19:08, 21 February 2008

File:2nn6.jpg


2nn6, resolution 3.35Å

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Structure of the human RNA exosome composed of Rrp41, Rrp45, Rrp46, Rrp43, Mtr3, Rrp42, Csl4, Rrp4, and Rrp40

OverviewOverview

The RNA exosome is a multisubunit 3' to 5' exoribonuclease complex that participates in degradation and processing of cellular RNA. To determine the activities and structure of the eukaryotic exosome, we report the reconstitution of 9-subunit exosomes from yeast and human and reconstitution of 10- and 11-subunit exosomes from yeast. Comparative biochemical analysis between purified subunits and reconstituted exosomes using AU-rich, polyadenylated (poly[A]), generic, and structured RNA substrates reveals processive phosphorolytic activities for human Rrp41/Rrp45 and the 9-subunit human exosome, processive hydrolytic activities for yeast Rrp44 and the yeast 10-subunit exosome, distributive hydrolytic activities for Rrp6, and processive and distributive hydrolytic activities for the yeast 11-subunit exosome. To elucidate the architecture of a eukaryotic exosome, its conserved surfaces, and the structural basis for RNA decay, we report the X-ray structure determination for the 286 kDa nine-subunit human exosome at 3.35 A.

About this StructureAbout this Structure

2NN6 is a Protein complex structure of sequences from Homo sapiens. The following page contains interesting information on the relation of 2NN6 with [Exosomes]. Full crystallographic information is available from OCA.

ReferenceReference

Reconstitution, activities, and structure of the eukaryotic RNA exosome., Liu Q, Greimann JC, Lima CD, Cell. 2006 Dec 15;127(6):1223-37. PMID:17174896

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