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Literature summary for 3.6.5.3 extracted from

  • Li, W.; Liu, Z.; Koripella, R.K.; Langlois, R.; Sanyal, S.; Frank, J.
    Activation of GTP hydrolysis in mRNA-tRNA translocation by elongation factor G (2015), Sci. Adv., 1, e1500169 .
    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 conserved residue His91 plays a direct role in the switch II loop of EF-G in GTPase activation Escherichia coli

Protein Variants

Protein Variants Comment Organism
H91A the mutant of EF-G renders the enzyme impaired in GTP hydrolysis and thereby stabilizes it on the ribosome Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information single-turnover GTP hydrolysis kinetics by mixing 70S ribosomes and [3H]GTP with EF-G Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
ribosome
-
 Escherichia coli 5840
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP + H2O Escherichia coli
-
 GDP + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6M8
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + H2O
-
 Escherichia coli GDP + phosphate
-
 ?
additional information contacts between EF-G, protein S12, and helices 43 and 44 of 23S ribosomal RNA. Escherichia coli strain MRE600 70S ribosomes are used as substrates Escherichia coli ?
-
-

Synonyms

Synonyms Comment Organism
EF-G
-
 Escherichia coli
elongation factor G
-
 Escherichia coli
GTPase
-
 Escherichia coli
guanosine triphosphatase
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2 8 GTP recombinant enzyme EF-G mutant H91A, pH 7.5, 37°C Escherichia coli
202
-
 GTP wild-type enzyme EF-G, pH 7.5, 37°C Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Escherichia coli

General Information

General Information Comment Organism
malfunction EF-G mutant H91A hydrolyzes GTP at a substantially slower rate compared to wild-type EF-G Escherichia coli
additional information cryogenic electron microscopy (cryo-EM) at near-atomic resolution at 4.0-5.7 A resolution is used to investigate two complexes formed by EF-G H91A in its GTP-bound state with the ribosome, distinguished by the presence or absence of the intersubunit rotation, overview. GTP hydrolysis cannot proceed with EF-G bound to the unrotated form of the ribosome. Contacts between EF-G, protein S12, and helices 43 and 44 of 23S ribosomal RNA Escherichia coli
physiological function GTP hydrolysis in mRNA-tRNA translocation is catalyzed by elongation factor G, EF-G. GTP hydrolysis cannot proceed with EF-G bound to the unrotated form of the ribosome Escherichia coli