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Literature summary for 3.6.5.3 extracted from
- Molecular complementarity between tetracycline and the GTPase active site of elongation factor Tu (2006), Acta Crystallogr. Sect. D, 62, 1392-1400.
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | elongation factor Tu may have in vivo role in tetracycline inhibition of protein synthesis | Escherichia coli |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| two crystal forms of a complex between trypsin-modified elongation factor Tu-MgGDP and the antibiotic tetracycline solved by X-ray diffraction analysis to resolution of 2.8 and 2.1 A, respectively | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| EF-Tu | - |
Escherichia coli |
| elongation factor Tu | - |
Escherichia coli |
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