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Purification and crystallization of the ternary complex of elongation factor Tu:GTP and Phe‐tRNA Phe
Author(s) -
Nissen Poul,
Reshetnikova Ludmila,
Siboska Gunhild,
Polekhina Galina,
Thirup Søren,
Kjeldgaard Morten,
Clark Brian F.C.,
Nyborg Jens
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01254-7
Subject(s) - ef tu , ternary complex , gtp' , transfer rna , elongation factor , guanosine triphosphate , guanosine , biochemistry , gtpase , ribosome , chemistry , biology , rna , gene , enzyme
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.