2W1O

NMR structure of dimerization domain of human ribosomal protein P2

2W1O の概要

• エントリーDOI: 10.2210/pdb2w1o/pdb
• 関連するPDBエントリー: 1S4J
• 分子名称: 60S ACIDIC RIBOSOMAL PROTEIN P2 (1 entity in total)
• 機能のキーワード: ribosomal protein, ribonucleoprotein, ribosome, translation, dimerization, phosphoprotein
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 14414.37

構造登録者

Lee, K.M.,Chan, D.S.,Sze, K.H.,Zhu, G.,Shaw, P.C.,Wong, K.B. (登録日: 2008-10-20, 公開日: 2009-11-17, 最終更新日: 2024-05-15)

主引用文献

Lee, K.M.,Yu, C.W.,Chan, D.S.,Chiu, T.Y.,Zhu, G.,Sze, K.H.,Shaw, P.C.,Wong, K.B.
Solution Structure of the Dimerization Domain of Ribosomal Protein P2 Provides Insights for the Structural Organization of Eukaryotic Stalk.
Nucleic Acids Res., 38:5206-, 2010

PubMed Abstract: The lateral stalk of ribosome is responsible for kingdom-specific binding of translation factors and activation of GTP hydrolysis that drives protein synthesis. In eukaryotes, the stalk is composed of acidic ribosomal proteins P0, P1 and P2 that constitute a pentameric P-complex in 1: 2: 2 ratio. We have determined the solution structure of the N-terminal dimerization domain of human P2 (NTD-P2), which provides insights into the structural organization of the eukaryotic stalk. Our structure revealed that eukaryotic stalk protein P2 forms a symmetric homodimer in solution, and is structurally distinct from the bacterial counterpart L12 homodimer. The two subunits of NTD-P2 form extensive hydrophobic interactions in the dimeric interface that buries 2400 A(2) of solvent accessible surface area. We have showed that P1 can dissociate P2 homodimer spontaneously to form a more stable P1/P2 1 : 1 heterodimer. By homology modelling, we identified three exposed polar residues on helix-3 of P2 are substituted by conserved hydrophobic residues in P1. Confirmed by mutagenesis, we showed that these residues on helix-3 of P1 are not involved in the dimerization of P1/P2, but instead play a vital role in anchoring P1/P2 heterodimer to P0. Based on our results, models of the eukaryotic stalk complex were proposed.

PubMed: 20385603
DOI: 10.1093/NAR/GKQ231

実験手法

SOLUTION NMR