| Literature DB >> 27196944 |
Sergey Melnikov1,2, Justine Mailliot1,2, Byung-Sik Shin3, Lukas Rigger4, Gulnara Yusupova1,2, Ronald Micura4, Thomas E Dever3, Marat Yusupov1,2.
Abstract
Eukaryotic translation initiation factor eIF5A promotes protein synthesis by resolving polyproline-induced ribosomal stalling. Here, we report a 3.25-Å resolution crystal structure of eIF5A bound to the yeast 80S ribosome. The structure reveals a previously unseen conformation of an eIF5A-ribosome complex and highlights a possible functional link between conformational changes of the ribosome during protein synthesis and the eIF5A-ribosome association.Entities:
Keywords: crystallography; eIF5A; hypusine; ribosome; structure
Mesh:
Substances:
Year: 2016 PMID: 27196944 PMCID: PMC5408928 DOI: 10.1016/j.jmb.2016.05.011
Source DB: PubMed Journal: J Mol Biol ISSN: 0022-2836 Impact factor: 5.469