PMID:10368282
| Citation |
Nissen, P, Thirup, S, Kjeldgaard, M and Nyborg, J (1999) The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA. Structure 7:143-56 |
|---|---|
| Abstract |
. The translation elongation factor EF-Tu in its GTP-bound state forms a ternary complex with any aminoacylated tRNA (aa-tRNA), except initiator tRNA and selenocysteinyl-tRNA. This complex delivers aa-tRNA to the ribosomal A site during the elongation cycle of translation. The crystal structure of the yeast Phe-tRNAPhe ternary complex with Thermus aquaticus EF-Tu-GDPNP (Phe-TC) has previously been determined as one representative of this general yet highly discriminating complex formation. |
| Links | |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Crystallography, X-Ray; Escherichia coli/chemistry; GTP Phosphohydrolase-Linked Elongation Factors/chemistry; Guanosine Triphosphate/chemistry; Models, Molecular; Molecular Sequence Data; Nucleic Acid Conformation; Peptide Elongation Factor Tu/chemistry; Protein Conformation; RNA, Bacterial/chemistry; RNA, Transfer, Cys/chemistry; RNA, Transfer, Phe/chemistry; RNA-Binding Proteins/chemistry; Sequence Alignment; Thermus/chemistry |
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