7VB2

Solution structure of human ribosomal protein uL11

7VB2 の概要

• エントリーDOI: 10.2210/pdb7vb2/pdb
• 分子名称: 60S ribosomal protein L12 (1 entity in total)
• 機能のキーワード: ribosomal protein, translation, elongation factors
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17847.62

構造登録者

Lee, K.M.,Wong, K.B. (登録日: 2021-08-30, 公開日: 2022-04-20, 最終更新日: 2024-05-15)

主引用文献

Yang, L.,Lee, K.M.,Yu, C.W.,Imai, H.,Choi, A.K.,Banfield, D.K.,Ito, K.,Uchiumi, T.,Wong, K.B.
The flexible N-terminal motif of uL11 unique to eukaryotic ribosomes interacts with P-complex and facilitates protein translation.
Nucleic Acids Res., 50:5335-5348, 2022

PubMed Abstract: Eukaryotic uL11 contains a conserved MPPKFDP motif at the N-terminus that is not found in archaeal and bacterial homologs. Here, we determined the solution structure of human uL11 by NMR spectroscopy and characterized its backbone dynamics by 15N-1H relaxation experiments. We showed that these N-terminal residues are unstructured and flexible. Structural comparison with ribosome-bound uL11 suggests that the linker region between the N-terminal domain and C-terminal domain of human uL11 is intrinsically disordered and only becomes structured when bound to the ribosomes. Mutagenesis studies show that the N-terminal conserved MPPKFDP motif is involved in interacting with the P-complex and its extended protuberant domain of uL10 in vitro. Truncation of the MPPKFDP motif also reduced the poly-phenylalanine synthesis in both hybrid ribosome and yeast mutagenesis studies. In addition, G→A/P substitutions to the conserved GPLG motif of helix-1 reduced poly-phenylalanine synthesis to 9-32% in yeast ribosomes. We propose that the flexible N-terminal residues of uL11, which could extend up to ∼25 Å from the N-terminal domain of uL11, can form transient interactions with the uL10 that help to fetch and fix it into a position ready for recruiting the incoming translation factors and facilitate protein synthesis.

PubMed: 35544198
DOI: 10.1093/nar/gkac292

実験手法

SOLUTION NMR