Ilkin Yapici1, Hasan DeMirci1,2
1Department of Molecular Biology and Genetics, Koc University, 34450, Istanbul, Turkey
2Stanford PULSE Institute, SLAC National Laboratory, 94025, Menlo Park, CA, USA
Among the four phases of translation, initiation is the first, most rate-limiting, and most complicated translational phase. The binding of initiation factor 1 (IF-1) to the 30S ribosomal subunit is one of the most crucial steps to form a fully assembled translating ribosome, and its atomic details remain elusive. Thanks to X-ray Free Electron Lasers, we managed to observe the molecular details of protein-RNA and protein-protein interactions at atomic resolution in real-time. Our data illustrate the missing links between initial IF-1 interaction with critical decoding residues A1492 and A1493 from 16S RNA and enable us to observe conformational changes caused in the 30S subunit at hitherto time scales and resolution.
Keywords: structural dynamics; structural biology; crystallography; ribosome; time-resolved crystallography