2HBK

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

Summary for 2HBK

• Entry DOI: 10.2210/pdb2hbk/pdb
• Related: 2HBJ 2HBL 2HBM
• Descriptor: Exosome complex exonuclease RRP6, MANGANESE (II) ION (3 entities in total)
• Functional Keywords: exosome, rna metabolism, rna surveillance, rna processing, hydrolase, gene regulation
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Nucleus, nucleolus : Q12149
• Total number of polymer chains: 1
• Total formula weight: 47785.00

Authors

Midtgaard, S.F.,Assenholt, J.,Jonstrup, A.T.,Van, L.B.,Jensen, T.H.,Brodersen, D.E. (deposition date: 2006-06-14, release date: 2006-07-25, Last modification date: 2023-10-25)

Primary citation

Midtgaard, S.F.,Assenholt, J.,Jonstrup, A.T.,Van, L.B.,Jensen, T.H.,Brodersen, D.E.
Structure of the nuclear exosome component Rrp6p reveals an interplay between the active site and the HRDC domain.
Proc.Natl.Acad.Sci.Usa, 103:11898-11903, 2006

PubMed Abstract: 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.

PubMed: 16882719
DOI: 10.1073/pnas.0604731103

Experimental method

X-RAY DIFFRACTION (2.25 Å)