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Literature summary for 3.6.5.3 extracted from

  • Voorhees, R.; Schmeing, T.; Kelley, A.; Ramakrishnan, V.
    The mechanism for activation of GTP hydrolysis on the ribosome (2010), Science, 330, 835-838.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.5.3

Crystallization (Commentary)

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Thermus thermophilus
-
-
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
EF-Tu
-
 Thermus thermophilus
elongation factor Tu
-
 Thermus thermophilus

General Information

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