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Literature summary 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

Activating Compound

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

Cloned(Commentary)

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

Localization

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.5.3 Mg2+ required Thermus thermophilus

Natural Substrates/ Products (Substrates)

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
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.6.5.3 Thermus thermophilus Q5SKA7
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.5.3 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)

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 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

EC Number Synonyms Comment Organism
3.6.5.3 EF4
-
 Thermus thermophilus
3.6.5.3 elongation factor 4
-
 Thermus thermophilus
3.6.5.3 LepA
-
 Thermus thermophilus

General Information

EC Number General Information Comment Organism
3.6.5.3 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