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3JCN

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

This is a non-PDB format compatible entry.
Summary for 3JCN
Entry DOI10.2210/pdb3jcn/pdb
Related3JCJ
EMDB information3285 6559
Descriptor50S ribosomal protein L32, 50S ribosomal protein L4, 50S ribosomal protein L5, ... (57 entities in total)
Functional Keywordsribosome, translation initiation, gtpase, 70s, bacterial ribosome, if2, initiation factor 2
Biological sourceEscherichia coli
More
Total number of polymer chains55
Total formula weight2271067.66
Authors
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. (deposition date: 2016-01-04, release date: 2016-03-09, Last modification date: 2018-07-18)
Primary citationSprink, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.6 Å)
Structure validation

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