4beh

Solution structure of human ribosomal protein P1.P2 heterodimer

spinqualitylabelsall models 4beh Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4beh is a 2 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RLA1_HUMAN Plays an important role in the elongation step of protein synthesis.[HAMAP-Rule:MF_01478] Publication Abstract from PubMed 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 approximately 125 A away from the dimerization domains. 15N 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. Solution structure of human P1*P2 heterodimer provides insights into the role of eukaryotic stalk in recruiting the ribosome-inactivating protein trichosanthin to the ribosome.,Lee KM, Yusa K, Chu LO, Wing-Heng Yu C, Oono M, Miyoshi T, Ito K, Shaw PC, Wong KB, Uchiumi T Nucleic Acids Res. 2013 Jul 26. PMID:23892290 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribosomal protein P1 Ribosomal protein P2

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