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Literature summary for 3.6.5.3 extracted from

  • Kumar, V.; Ero, R.; Ahmed, T.; Goh, K.J.; Zhan, Y.; Bhushan, S.; Gao, Y.G.
    Structure of the GTP form of elongation factor 4 (EF4) bound to the ribosome (2016), J. Biol. Chem., 291, 12943-12950 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.5.3

Activating Compound

Activating Compound Comment Organism Structure
additional information EF4 GTPase activation upon ribosome binding Thermus thermophilus

Cloned(Commentary)

Cloned (Comment) Organism
gene lepA, recombinant expression of N-terminally His6-tagged enzyme EF4 in Escherichia coli strain BL21(DE3) Rosetta T1R Thermus thermophilus

Localization

Localization Comment Organism GeneOntology No. Textmining
ribosome
-
 Thermus thermophilus 5840
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required 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
-
 ?

Organism

Organism UniProt Comment Textmining
Thermus thermophilus Q5SKA7
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally His6-tagged enzyme EF4 from Escherichia coli strain BL21(DE3) Rosetta T1R by nickel affinity chromatography, cleavage of the His-tag, followed by gel filtration and anion exchange chromatography Thermus thermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + H2O
-
 Thermus thermophilus GDP + phosphate
-
 ?
additional information the G-nucleotide binding pocket includes five G motifs (G1-G5) that are conserved in trGTPase factors. In the ribosome-bound EF4, the G1 motif (residues 18-24) establishes extensive contacts with the triphosphate moiety and ribose sugar of GDPCP. EF4 GTPase activation upon ribosome binding Thermus thermophilus ?
-
-

Synonyms

Synonyms Comment Organism
EF4
-
 Thermus thermophilus
elongation factor 4
-
 Thermus thermophilus
LepA
-
 Thermus thermophilus

General Information

General Information Comment Organism
additional information structure of the GTP form of elongation factor 4 (EF4) bound to ribosome 50S and 30S subunits with tRNA in the P and E sites, single-particle cryo-electron microscopy and modeling, overview. The superposition of this structure with that of the crystal structure of EF4-GDP bound to the ribosome by aligning on the 23S rRNA clearly shows the different orientations of EF4 in the ribosome. A conformational change of EF4 occurs upon ribosome binding and GTP hydrolysis, the unique domains (domain IV in EF-G and CTD in EF4) are positioned in completely different orientations relative to the shared domains, structure comparison with elongation factor G (EF-G) Thermus thermophilus