2JA9

Structure of the N-terminal deletion of yeast exosome component Rrp40

2JA9 の概要

• エントリーDOI: 10.2210/pdb2ja9/pdb
• 分子名称: EXOSOME COMPLEX EXONUCLEASE RRP40 (2 entities in total)
• 機能のキーワード: rna-binding protein, rna, exosome, nuclease, s1 domain, kh domain, hydrolase, rna-binding, exonuclease, nuclear protein, rrna processing, nucleic-acid binding, rna binding protein
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKERS' YEAST)
• 細胞内の位置: Cytoplasm: Q08285
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19607.51

構造登録者

Oddone, A.,Lorentzen, E.,Basquin, J.,Gasch, A.,Rybin, V.,Conti, E.,Sattler, M. (登録日: 2006-11-24, 公開日: 2006-12-13, 最終更新日: 2024-05-08)

主引用文献

Oddone, A.,Lorentzen, E.,Basquin, J.,Gasch, A.,Rybin, V.,Conti, E.,Sattler, M.
Structural and Biochemical Characterization of the Yeast Exosome Component Rrp40
Embo Rep., 8:63-, 2007

PubMed Abstract: The exosome is a protein complex that is important in both degradation and 3'-processing of eukaryotic RNAs. We present the crystal structure of the Rrp40 exosome subunit from Saccharomyces cerevisiae at a resolution of 2.2 A. The structure comprises an S1 domain and an unusual KH (K homology) domain. Close packing of the S1 and KH domains is stabilized by a GxNG sequence, which is uniquely conserved in exosome KH domains. Nuclear magnetic resonance data reveal the presence of a manganese-binding site at the interface of the two domains. Isothermal titration calorimetry shows that Rrp40 and archaeal Rrp4 alone have very low intrinsic affinity for RNA. The affinity of an archaeal core exosome for RNA is significantly increased in the presence of the S1-KH subunit Rrp4, indicating that multiple subunits might contribute to cooperative binding of RNA substrates by the exosome.

PubMed: 17159918
DOI: 10.1038/SJ.EMBOR.7400856

実験手法

X-RAY DIFFRACTION (2.2 Å)