3JCN

Structures of ribosome-bound initiation factor 2 reveal the mechanism of subunit association: Initiation Complex I

これはPDB形式変換不可エントリーです。

3JCN の概要

• エントリーDOI: 10.2210/pdb3jcn/pdb
• 関連するPDBエントリー: 3JCJ
• EMDBエントリー: 3285 6559
• 分子名称: 50S ribosomal protein L32, 50S ribosomal protein L4, 50S ribosomal protein L5, ... (57 entities in total)
• 機能のキーワード: ribosome, translation initiation, gtpase, 70s, bacterial ribosome, if2, initiation factor 2
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 55
• 化学式量合計: 2271067.66

構造登録者

Sprink, T.,Ramrath, D.J.F.,Yamamoto, H.,Yamamoto, K.,Loerke, J.,Ismer, J.,Hildebrand, P.W.,Scheerer, P.,Buerger, J.,Mielke, T.,Spahn, C.M.T. (登録日: 2016-01-04, 公開日: 2016-03-09, 最終更新日: 2018-07-18)

主引用文献

Sprink, T.,Ramrath, D.J.,Yamamoto, H.,Yamamoto, K.,Loerke, J.,Ismer, J.,Hildebrand, P.W.,Scheerer, P.,Burger, J.,Mielke, T.,Spahn, C.M.
Structures of ribosome-bound initiation factor 2 reveal the mechanism of subunit association.
Sci Adv, 2:e1501502-e1501502, 2016

PubMed Abstract: Throughout the four phases of protein biosynthesis-initiation, elongation, termination, and recycling-the ribosome is controlled and regulated by at least one specified translational guanosine triphosphatase (trGTPase). Although the structural basis for trGTPase interaction with the ribosome has been solved for the last three steps of translation, the high-resolution structure for the key initiation trGTPase, initiation factor 2 (IF2), complexed with the ribosome, remains elusive. We determine the structure of IF2 complexed with a nonhydrolyzable guanosine triphosphate analog and initiator fMet-tRNAi (Met) in the context of the Escherichia coli ribosome to 3.7-Å resolution using cryo-electron microscopy. The structural analysis reveals previously unseen intrinsic conformational modes of the 70S initiation complex, establishing the mutual interplay of IF2 and initator transfer RNA (tRNA) with the ribsosome and providing the structural foundation for a mechanistic understanding of the final steps of translation initiation.

PubMed: 26973877
DOI: 10.1126/sciadv.1501502

実験手法

ELECTRON MICROSCOPY (4.6 Å)