PMID:8939739

Citation	Polekhina, G, Thirup, S, Kjeldgaard, M, Nissen, P, Lippmann, C and Nyborg, J (1996) Helix unwinding in the effector region of elongation factor EF-Tu-GDP. Structure 4:1141-51
Abstract	Elongation factor Tu (EF-Tu) in its GTP conformation is a carrier of aminoacylated tRNAs (aa-tRNAs) to the ribosomal A site during protein biosynthesis. The ribosome triggers GTP hydrolysis, resulting in the dissociation of EF-Tu-GDP from the ribosome. The affinity of EF-Tu for other molecules involved in this process, some of which are unknown, is regulated by two regions (Switch I and Switch II) that have different conformations in the GTP and GDP forms. The structure of the GDP form of EF-Tu is known only as a trypsin-modified fragment, which lacks the Switch I, or effector, domain. The aim of this work was to establish the overall structure of intact EF-Tu-GDP, in particular the structure of the effector domain.
Links	PubMed
Keywords	Bacterial Proteins/chemistry; Binding Sites; Computer Simulation; Crystallography; Escherichia coli; Guanosine Diphosphate/chemistry; Models, Molecular; Molecular Sequence Data; Peptide Elongation Factor Tu/chemistry; Protein Structure, Secondary; Species Specificity; Thermus
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