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Literature summary for 3.6.5.3 extracted from

  • Nguyen, B.; Ticu, C.; Wilson, K.S.
    Intramolecular movements in EF-G, trapped at different stages in its GTP hydrolytic cycle, probed by FRET (2010), J. Mol. Biol., 397, 1245-1260.
    View publication on PubMed
Search for more literature for 3.6.5.3

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of EF-G mutants 58C and 196C Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information two EF-G cysteine mutants 58C and 196C react efficiently with 2',7'-difluorofluorescein maleimide, whereas the cysteine-free protein is unreactive Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
additional information viomycin and fusidic acid do not prevent GTP hydrolysis, but these antibiotics trap EF-G on the ribosome before or after ribosomal translocation, respectively Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information ribosome binding kinetics of GTP hydrolysis-inactive recombinant EF-G mutants 58C and 196C labeled with 2',7'-difluorofluorescein maleimide, i.e. 58C-mant and 196C-mant, overview 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
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant EF-G mutants 58C and 196C Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2',3'-O-N'-methylanthranilate-GTP + H2O 2',3'-O-N'-methylanthranilate, i.e. mant, is attached to GTP. EF-G binds and efficiently hydrolyzes mant-GTP in a ribosome-dependent manner Escherichia coli 2',3'-O-N'-methylanthranilate-GDP + phosphate
-
 ?
GTP + H2O
-
 Escherichia coli GDP + phosphate
-
 ?
additional information residue 196 is located in a solvent-exposed location of the G' subdomain, while its neighboring helices AG' and BG' make contacts with protein L7/L12 of the ribosome. The latter contacts involve conserved electrostatically interacting residues that allosterically activate GTP hydrolysis in the G domain of EF-G. Residue 58 moves substantially from its initial ordered position adjacent to helix BIII Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
EF-G
-
 Escherichia coli
elongation factor G
-
 Escherichia coli

General Information

General Information Comment Organism
additional information cyclical movements of switch element I, sw1, within EF-G, Sw1 exposure depends on EF-G functional state, conformational changes in sw1 help to drive the unidirectional EF-G cycle during protein synthesis, intramolecular movements in EF-G, overview Escherichia coli
physiological function elongation factor G, EF-G, is one of several GTP hydrolytic proteins that cycles repeatedly on and off the ribosome during protein synthesis in bacterial cells. In the functional cycle of EF-G, hydrolysis of GTP is coupled to tRNA-mRNA translocation in ribosomes. GTP hydrolysis induces conformational rearrangements in two switch elements in the G domain of EF-G and other GTPases. These switch elements are thought to initiate the cascade of events that lead to translocation and EF-G cycling between ribosomes, coupling mechanism, overview Escherichia coli