2W1O
NMR structure of dimerization domain of human ribosomal protein P2
Summary for 2W1O
| Entry DOI | 10.2210/pdb2w1o/pdb |
| Related | 1S4J |
| Descriptor | 60S ACIDIC RIBOSOMAL PROTEIN P2 (1 entity in total) |
| Functional Keywords | ribosomal protein, ribonucleoprotein, ribosome, translation, dimerization, phosphoprotein |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 2 |
| Total formula weight | 14414.37 |
| Authors | Lee, K.M.,Chan, D.S.,Sze, K.H.,Zhu, G.,Shaw, P.C.,Wong, K.B. (deposition date: 2008-10-20, release date: 2009-11-17, Last modification date: 2024-05-15) |
| Primary citation | 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 Cited by 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: 20385603DOI: 10.1093/NAR/GKQ231 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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