EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.6.5.3 | H91A | a GTPase-defective EF-G mutant | Escherichia coli |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.6.5.3 | Fusidic acid | - |
Escherichia coli | |
3.6.5.3 | Fusidic acid | - |
Thermus thermophilus | |
3.6.5.3 | additional information | in free enzyme EF-G, crucial sensors of switch I and II regions are disordered and become ordered in the complex with a nonhydrolyzable GTP analogue, GDPCP, on the ribosome. This causes a reorientation of EF-G such that the tip of domain IV moves and the CHI state ofthe ribosome is stabilized | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.6.5.3 | GTP + H2O | Thermus thermophilus | - |
GDP + phosphate | - |
? | |
3.6.5.3 | GTP + H2O | Escherichia coli | - |
GDP + phosphate | - |
? | |
3.6.5.3 | additional information | Escherichia coli | EF-G binding, without GTP hydrolysis, promotes slow and possibly incomplete translocation | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.6.5.3 | Escherichia coli | - |
- |
- |
3.6.5.3 | Thermus thermophilus | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.6.5.3 | GTP + H2O = GDP + phosphate | reaction mechanism, overview | Thermus thermophilus | |
3.6.5.3 | GTP + H2O = GDP + phosphate | reaction mechanism, overview | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.6.5.3 | GTP + H2O | - |
Thermus thermophilus | GDP + phosphate | - |
? | |
3.6.5.3 | GTP + H2O | - |
Escherichia coli | GDP + phosphate | - |
? | |
3.6.5.3 | additional information | EF-G binding, without GTP hydrolysis, promotes slow and possibly incomplete translocation | Escherichia coli | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.6.5.3 | EF-G | - |
Escherichia coli |
3.6.5.3 | EF-Tu | - |
Thermus thermophilus |
3.6.5.3 | elongation factor G | - |
Thermus thermophilus |
3.6.5.3 | elongation factor G | - |
Escherichia coli |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.6.5.3 | additional information | overall scheme of translocation: in the pre-translocation state, deacylated tRNA is bound in the P site and peptidy-tRNAl in the A site, both bound to their cognate codons in the mRNA. Following the binding of EF-G-GTP to the pretranslocation complex, translocation takes place. In the post-translocation state, peptidyl-tRNA has moved to the P site, whereas deacylated tRNA has dissociated, as have inorganic phosphate and EF-G-GDP. A histidine residue in the switch II region, His84 in Thermus thermophilus EF-G, plays an essential role in the reaction, structure-function relationships, overview | Thermus thermophilus |
3.6.5.3 | additional information | overall scheme of translocation: in the pre-translocation state, deacylated tRNA is bound in the P site and peptidy-tRNAl in the A site, both bound to their cognate codons in the mRNA. Following the binding of EF-G-GTP to the pretranslocation complex, translocation takes place. In the post-translocation state, peptidyl-tRNA has moved to the P site, whereas deacylated tRNA has dissociated, as have inorganic phosphate and EF-G-GDP. A histidine residue in the switch II region, His91 in Escherichia coli EF-G, plays an essential role in the reaction, structure-function relationships, overview | Escherichia coli |
3.6.5.3 | physiological function | synchronous tRNA movements during translocation on the ribosome are orchestrated by elongation factor G and GTP hydrolysis | Thermus thermophilus |
3.6.5.3 | physiological function | synchronous tRNA movements during translocation on the ribosome are orchestrated by elongation factor G and GTP hydrolysis | Escherichia coli |