2VAZ

Model of the S15-mRNA complex fitted into the cryo-EM map of the 70S entrapment complex.

2VAZ の概要

• エントリーDOI: 10.2210/pdb2vaz/pdb
• 関連するPDBエントリー: 1P6G 1P87 2AVY 2AW7
• EMDBエントリー: 1391
• 分子名称: RPSO MRNA OPERATOR, 30S RIBOSOMAL PROTEIN S15 (2 entities in total)
• 機能のキーワード: translation, platform-binding center, gene expression regulation, ribosomal protein, ribonucleoprotein, protein synthesis, translation initiation, ribosome, riboswitch, rna-binding, rrna-binding, rna pseudoknot, mrna structure, repressor protein
• 由来する生物種: ESCHERICHIA COLI; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 69717.93

構造登録者

Marzi, S.,Myasnikov, A.G.,Serganov, A.,Ehresmann, C.,Romby, P.,Yusupov, M.,Klaholz, B.P. (登録日: 2007-09-05, 公開日: 2007-10-02, 最終更新日: 2024-05-08)

主引用文献

Marzi, S.,Myasnikov, A.G.,Serganov, A.,Ehresmann, C.,Romby, P.,Yusupov, M.,Klaholz, B.P.
Structured Mrnas Regulate Translation Initiation by Binding to the Platform of the Ribosome.
Cell(Cambridge,Mass.), 130:1019-, 2007

PubMed Abstract: Gene expression can be regulated at the level of initiation of protein biosynthesis via structural elements present at the 5' untranslated region of mRNAs. These folded mRNA segments may bind to the ribosome, thus blocking translation until the mRNA unfolds. Here, we report a series of cryo-electron microscopy snapshots of ribosomal complexes directly visualizing either the mRNA structure blocked by repressor protein S15 or the unfolded, active mRNA. In the stalled state, the folded mRNA prevents the start codon from reaching the peptidyl-tRNA (P) site inside the ribosome. Upon repressor release, the mRNA unfolds and moves into the mRNA channel allowing translation initiation. A comparative structure and sequence analysis suggests the existence of a universal stand-by site on the ribosome (the 30S platform) dedicated for binding regulatory 5' mRNA elements. Different types of mRNA structures may be accommodated during translation preinitiation and regulate gene expression by transiently stalling the ribosome.

PubMed: 17889647
DOI: 10.1016/J.CELL.2007.07.008

実験手法

ELECTRON MICROSCOPY (10 Å)