2HBL

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

2HBL の概要

• エントリーDOI: 10.2210/pdb2hbl/pdb
• 関連するPDBエントリー: 2HBJ 2HBK 2HBM
• 分子名称: Exosome complex exonuclease RRP6, ZINC ION, MANGANESE (II) ION, ... (5 entities in total)
• 機能のキーワード: exosome, rna metabolism, rna surveillance, rna processing, hydrolase, gene regulation
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Nucleus, nucleolus : Q12149
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48142.69

構造登録者

Midtgaard, S.F.,Assenholt, J.,Jonstrup, A.T.,Van, L.B.,Jensen, T.H.,Brodersen, D.E. (登録日: 2006-06-14, 公開日: 2006-07-25, 最終更新日: 2023-10-25)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.3 Å)