4BEH

Solution structure of human ribosomal protein P1.P2 heterodimer

Summary for 4BEH

• Entry DOI: 10.2210/pdb4beh/pdb
• NMR Information: BMRB: 19086
• Descriptor: 60S ACIDIC RIBOSOMAL PROTEIN P1, 60S ACIDIC RIBOSOMAL PROTEIN P2 (2 entities in total)
• Functional Keywords: stalk, ribosome, translation
• Biological source: HOMO SAPIENS (HUMAN); More
• Total number of polymer chains: 2
• Total formula weight: 23269.84

Authors

Lee, K.M.,Yusa, K.,Chu, L.O.,Wing-Heng Yu, C.,Shaw, P.C.,Oono, M.,Miyoshi, T.,Ito, K.,Wong, K.B.,Uchiumi, T. (deposition date: 2013-03-10, release date: 2013-08-14, Last modification date: 2024-06-19)

Primary citation

Lee, K.M.,Yusa, K.,Chu, L.O.,Wing-Heng Yu, C.,Oono, M.,Miyoshi, T.,Ito, K.,Shaw, P.C.,Wong, K.B.,Uchiumi, T.
Solution Structure of Human P1P2 Heterodimer Provides Insights Into the Role of Eukaryotic Stalk in Recruiting the Ribosome-Inactivating Protein Trichosanthin to the Ribosome.
Nucleic Acids Res., 41:8776-, 2013

PubMed Abstract: Lateral ribosomal stalk is responsible for binding and recruiting translation factors during protein synthesis. The eukaryotic stalk consists of one P0 protein with two copies of P1•P2 heterodimers to form a P0(P1•P2)₂ pentameric P-complex. Here, we have solved the structure of full-length P1•P2 by nuclear magnetic resonance spectroscopy. P1 and P2 dimerize via their helical N-terminal domains, whereas the C-terminal tails of P1•P2 are unstructured and can extend up to ∼125 Å away from the dimerization domains. (15)N relaxation study reveals that the C-terminal tails are flexible, having a much faster internal mobility than the N-terminal domains. Replacement of prokaryotic L10(L7/L12)₄/L11 by eukaryotic P0(P1•P2)₂/eL12 rendered Escherichia coli ribosome, which is insensitive to trichosanthin (TCS), susceptible to depurination by TCS and the C-terminal tail was found to be responsible for this depurination. Truncation and insertion studies showed that depurination of hybrid ribosome is dependent on the length of the proline-alanine rich hinge region within the C-terminal tail. All together, we propose a model that recruitment of TCS to the sarcin-ricin loop required the flexible C-terminal tail, and the proline-alanine rich hinge region lengthens this C-terminal tail, allowing the tail to sweep around the ribosome to recruit TCS.

PubMed: 23892290
DOI: 10.1093/NAR/GKT636

Experimental method

SOLUTION NMR