Crystallization (Comment) | Organism |
---|---|
EF-Tu bound to aminoacyl-tRNA of the 70s ribosome and a GTP analogue, X-ray diffraction structure determination and analysis at 3.1 A resolution | Thermus thermophilus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
GTP + H2O | Thermus thermophilus | - |
GDP + phosphate | - |
? | |
GTP + H2O | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | - |
GDP + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermus thermophilus | - |
- |
- |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
GTP + H2O | - |
Thermus thermophilus | GDP + phosphate | - |
? | |
GTP + H2O | EF-Tu is in its active conformation, when the switch I loop is ordered, and the catalytic histidine is coordinating the nucleophilic water in position for inline attack on the gamma-phosphate of GTP. The activated conformation is achieved due to a critical and conserved interaction of the histidine with A2662 of the sarcin-ricin loop of the 23S ribosomal RNA. Universal mechanism for GTPase activation and hydrolysis in translational GTPases on the ribosome. Premature GTP hydrolysis in EF-Tu is prevented by a hydrophobic gate consisting of residues Val20 of the P loop and Ile60 of switch I, which restricts access of His84 to the catalytic water | Thermus thermophilus | GDP + phosphate | - |
? | |
GTP + H2O | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | GDP + phosphate | - |
? | |
GTP + H2O | EF-Tu is in its active conformation, when the switch I loop is ordered, and the catalytic histidine is coordinating the nucleophilic water in position for inline attack on the gamma-phosphate of GTP. The activated conformation is achieved due to a critical and conserved interaction of the histidine with A2662 of the sarcin-ricin loop of the 23S ribosomal RNA. Universal mechanism for GTPase activation and hydrolysis in translational GTPases on the ribosome. Premature GTP hydrolysis in EF-Tu is prevented by a hydrophobic gate consisting of residues Val20 of the P loop and Ile60 of switch I, which restricts access of His84 to the catalytic water | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | GDP + phosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
EF-Tu | - |
Thermus thermophilus |
elongation factor Tu | - |
Thermus thermophilus |
General Information | Comment | Organism |
---|---|---|
metabolism | universal mechanism for GTPase activation and hydrolysis in translational GTPases on the ribosome | Thermus thermophilus |
physiological function | protein synthesis requires several GTPase factors, including elongation factor Tu, EF-Tu, which delivers aminoacyl-tRNAs to the ribosome | Thermus thermophilus |