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-Structure paper
タイトル | Structures of ribosome-bound initiation factor 2 reveal the mechanism of subunit association. |
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ジャーナル・号・ページ | Sci Adv, Vol. 2, Issue 3, Page e1501502, Year 2016 |
掲載日 | 2016年3月4日 |
著者 | Thiemo Sprink / David J F Ramrath / Hiroshi Yamamoto / Kaori Yamamoto / Justus Loerke / Jochen Ismer / Peter W Hildebrand / Patrick Scheerer / Jörg Bürger / Thorsten Mielke / Christian M T Spahn / |
PubMed 要旨 | 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 ...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. |
リンク | Sci Adv / PubMed:26973877 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.7 - 4.6 Å |
構造データ | |
化合物 | ChemComp-MG: ChemComp-ZN: ChemComp-GNP: ChemComp-FME: ChemComp-HOH: |
由来 |
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キーワード | RIBOSOME / translation initiation / translation initiation factor 2 / IF2 / translational GTPase / 70S / fMet-tRNA / GTPase / bacterial ribosome / initiation factor 2 |