title: Purification and crystallization of the ternary complex of elongation factor Tu:GTP and Phe-tRNA(Phe).
abstract: Elongation factor Tu (EF-Tu) is the most abundant protein in prokaryotic cells. Its general function in protein biosynthesis is well established. It is a member of the large family of G-proteins, all of which bind guanosine phosphates (GDP or GTP) as cofactors. In its active GTP bound state EF-Tu binds aminoacylated tRNA (aa-tRNA) forming the ternary complex EF-Tu:GTP:aa-tRNA. The ternary complex interacts with the ribosome where the anticodon on tRNA recognises a codon on mRNA, GTPase activity is induced and inactive EF-Tu:GDP is released. Here we report the successful crystallization of a ternary complex of Thermus aquaticus EF-Tu:GDPNP and yeast Phe-tRNA(Phe) after its purification by HPLC.
authors: Department of Biostructural Chemistry, University of Aarhus, Denmark.
authors: P
authors: P
authors: Nissen
authors: L
authors: L
authors: Reshetnikova
authors: G
authors: G
authors: Siboska
authors: G
authors: G
authors: Polekhina
authors: S
authors: S
authors: Thirup
authors: M
authors: M
authors: Kjeldgaard
authors: B F
authors: BF
authors: Clark
authors: J
authors: J
authors: Nyborg
mesh_terms: D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D006160:Guanosine Triphosphate / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D006165:Guanylyl Imidodiphosphate / Q000378:metabolism; D010444:Peptide Elongation Factor Tu / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D012360:RNA, Transfer, Phe / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D013824:Thermus / Q000378:metabolism
chemical_list: D012360:RNA, Transfer, Phe; D006165:Guanylyl Imidodiphosphate; D006160:Guanosine Triphosphate; D010444:Peptide Elongation Factor Tu