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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Nissen P,Reshetnikova L,Siboska G,Polekhina G,Thirup S,Kjeldgaard M,Clark BF,Nyborg Jdoi
10.1016/0014-5793(94)01254-7subject
Has Abstractpub_date
1994-12-19 00:00:00pages
165-8issue
2-3eissn
0014-5793issn
1873-3468pii
0014-5793(94)01254-7journal_volume
356pub_type
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