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  Structures of ribosome-bound initiation factor 2 reveal mechanism of subunit association

Sprink, T., Ramrath, D. J. F., Yamamoto, H., Yamamoto, K., Loerke, J., Ismer, J., et al. (2016). Structures of ribosome-bound initiation factor 2 reveal mechanism of subunit association. Science Advances, 2(3): e1501502. doi:10.1126/sciadv.1501502.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-44E0-F Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-44E1-D
Genre: Journal Article

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2016©The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science.

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 Creators:
Sprink, Thiemo1, Author
Ramrath, David J. F.1, Author
Yamamoto, Hiroshi 1, Author
Yamamoto, Kaori 1, Author
Loerke, Justus1, Author
Ismer, Jochen1, Author
Hildebrand, Peter W. 1, Author
Scheerer, Patrick1, Author
Bürger, Jörg1, 2, Author              
Mielke, Thorsten1, 2, Author              
Spahn, Christian M. T. , Author
Affiliations:
11Institut für Medizinische Physik und Biophysik, Charité–Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany, ou_persistent22              
2Microscopy and Cryo-Electron Microscopy (Head: Thorsten Mielke), Scientific Service (Head: Christoph Krukenkamp), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479668              

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Free keywords: protein biosynthesis, translational guanosine triphosphatase (trGTPase), structural biology
 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-tRNAiMet 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.

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Language(s): eng - English
 Dates: 2016-03-04
 Publication Status: Published online
 Pages: -
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 Identifiers: DOI: 10.1126/sciadv.1501502
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Title: Science Advances
  Other : Sci. Adv.
Source Genre: Journal
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Publ. Info: Washington : AAAS
Pages: - Volume / Issue: 2 (3) Sequence Number: e1501502 Start / End Page: - Identifier: Other: 2375-2548
CoNE: /journals/resource/2375-2548