4V4G

Crystal structure of five 70s ribosomes from Escherichia Coli in complex with protein Y.

これはPDB形式変換不可エントリーです。

4V4G の概要

• エントリーDOI: 10.2210/pdb4v4g/pdb
• 関連するPDBエントリー: 1VOR 1VOS 1VOU 1VOV 1VOW 1VOX 1VOY 1VOZ 1VP0
• 分子名称: 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (53 entities in total)
• 機能のキーワード: 30s ribosomal subunit, protein-rna complex, protein-protein complex, rna-rna complex, ribosome
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 265
• 化学式量合計: 10637746.99

構造登録者

Vila-Sanjurjo, A.,Schuwirth, B.S.,Hau, C.W.,Cate, J.H. (登録日: 2004-10-06, 公開日: 2014-07-09, 最終更新日: 2024-11-20)

主引用文献

Vila-Sanjurjo, A.,Schuwirth, B.S.,Hau, C.W.,Cate, J.H.
Structural basis for the control of translation initiation during stress.
Nat.Struct.Mol.Biol., 11:1054-1059, 2004

PubMed Abstract: During environmental stress, organisms limit protein synthesis by storing inactive ribosomes that are rapidly reactivated when conditions improve. Here we present structural and biochemical data showing that protein Y, an Escherichia coli stress protein, fills the tRNA- and mRNA-binding channel of the small ribosomal subunit to stabilize intact ribosomes. Protein Y inhibits translation initiation during cold shock but not at normal temperatures. Furthermore, protein Y competes with conserved translation initiation factors that, in bacteria, are required for ribosomal subunit dissociation. The mechanism used by protein Y to reduce translation initiation during stress and quickly release ribosomes for renewed translation initiation may therefore occur widely in nature.

PubMed: 15502846
DOI: 10.1038/nsmb850

実験手法

X-RAY DIFFRACTION (11.5 Å)