| + |
GTP | form complex 
binding
|
EEF1A:GTP:aa-tRNA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270812 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8722040 |
The mechanism of elongation factor Tu (EF-Tu) catalyzed aminoacyl-tRNA (aa-tRNA) binding to the A site of the ribosome was studied. Two types of complexes of EF-Tu with GTP and aa-tRNA, EF-Tu.GTP-aa-tRNA (ternary) and (EF-Tu.GTP)2.aa-tRNA (quinternary), can be formed in vitro depending on the conditions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Translation elongation and termination |
| + |
EEF1A1 | form complex
binding
|
EEF1A:GTP:aa-tRNA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270809 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8722040 |
The mechanism of elongation factor Tu (EF-Tu) catalyzed aminoacyl-tRNA (aa-tRNA) binding to the A site of the ribosome was studied. Two types of complexes of EF-Tu with GTP and aa-tRNA, EF-Tu.GTP-aa-tRNA (ternary) and (EF-Tu.GTP)2.aa-tRNA (quinternary), can be formed in vitro depending on the conditions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Translation elongation and termination |
| + |
EEF1A:GTP:aa-tRNA | up-regulates activity 
binding
|
80S_cytosolic_ribosome |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270810 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20025795 |
The work cycle during which a new amino acid is added to the growing polypeptide chain, referred to as elongation cycle, is a repetitive multistep process encompassing aminoacyl-tRNA (aa-tRNA) selection, peptide bond formation, and mRNA–tRNA translocation (Fig. 1). In the initial binding state, referred to as A/T state, this aa-tRNA is in a ternary complex with the GTPase EF-Tu (eEF1A in eukaryotes) and GTP. When a Watson–Crick codon–anticodon match is recognized by the ribosome, a signal is transmitted to EF-Tu that triggers GTP hydrolysis and thereby causes the dissociation of EF-Tu from the ribosome. The subsequent accommodation of the 3′ acceptor arm of the tRNA in the PTC of the large subunit leads to a rapid peptide bond transfer |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Translation elongation and termination |
| + |
alpha-aminoacyl-tRNA | form complex
binding
|
EEF1A:GTP:aa-tRNA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270808 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8722040 |
The mechanism of elongation factor Tu (EF-Tu) catalyzed aminoacyl-tRNA (aa-tRNA) binding to the A site of the ribosome was studied. Two types of complexes of EF-Tu with GTP and aa-tRNA, EF-Tu.GTP-aa-tRNA (ternary) and (EF-Tu.GTP)2.aa-tRNA (quinternary), can be formed in vitro depending on the conditions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Translation elongation and termination |
3.0
EEF1A:GTP:aa-tRNA