2hbk
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(New page: 200px<br /><applet load="2hbk" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hbk, resolution 2.250Å" /> '''Structure of the ye...)
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Revision as of 09:32, 21 November 2007
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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
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
2HBK is a Single protein structure of sequence from Saccharomyces cerevisiae with MN as ligand. 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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