the cryo-em structure of a complete 30s translation initiation complex from escherichia coli30年代的低温电子显微镜结构完整的翻译起始复合物从大肠杆菌.pdfVIP

The Cryo-EM Structure of a Complete 30S Translation Initiation Complex from Escherichia coli ´ 1 2 1 1 1 2 Patricia Julian , Pohl Milon , Xabier Agirrezabala , Gorka Lasso , David Gil , Marina V. Rodnina , Mikel Valle1,3* ´ 1 Structural Biology Unit, Center for Cooperative Research in Biosciences (CIC bioGUNE), Parque Tecnologico de Bizkaia, Derio, Spain, 2 Department of Physical ¨ Biochemistry, Max Planck Institute for Biophysical Chemistry, Gottingen, Germany, 3 Department of Biochemistry and Molecular Biology. Faculty of Science and Technology, University of the Basque Country, Bilbao, Spain Abstract Formation of the 30S initiation complex (30S IC) is an important checkpoint in regulation of gene expression. The selection of mRNA, correct start codon, and the initiator fMet-tRNAfMet requires the presence of three initiation factors (IF1, IF2, IF3) of which IF3 and IF1 control the fidelity of the process, while IF2 recruits fMet-tRNAfMet. Here we present a cryo-EM reconstruction of the complete 30S IC, containing mRNA, fMet-tRNAfMet, IF1, IF2, and IF3. In the 30S IC, IF2 contacts IF1, the 30S subunit shoulder, and the CCA end of fMet-tRNAfMet, which occupies a novel P/I position (P/I1). The N-terminal domain of IF3 contacts the tRNA, whereas the C-terminal domain is bound to the platform of the 30S subunit. Binding of initiation factors and fMet-tRNAfMet induces a rotation of the head relative to the body of the 30S subunit, which is