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Literature summary for 3.6.5.4 extracted from

  • Kempf, G.; Stjepanovic, G.; Sloan, J.; Hendricks, A.; Lapouge, K.; Sinning, I.
    The Escherichia coli SRP receptor forms a homodimer at the membrane (2018), Structure, 26, 1440-1450.e5 .
    View publication on PubMed
Search for more literature for 3.6.5.4

Activating Compound

Activating Compound Comment Organism Structure
additional information the FtsY GTPase is activated by formation of the targeting complex as well as upon membrane interaction, but homodimerization of FtsY also stimulates its GTPase activity Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information construction of the FtsYDELTAN1 mutant, and creation of a fusion construct comprising two FtsYDELTAN1 molecules linked via a 31-amino-acid GS linker, similar to the situation for the FtsY/Ffh heterodimer (FtsYDELTAN12) Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Escherichia coli 16020
-

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 P0AGD7 AND P10121 SRP receptor FtsY and the SRP protein Ffh
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + H2O
-
 Escherichia coli GDP + phosphate
-
 ?
additional information binding analysis of wild-type FtsY and mutant FtsYDELTAN1 with inactive GMPPNP substrate homologue, structure modeling, overview Escherichia coli ?
-
-

Subunits

Subunits Comment Organism
heterodimer
-
 Escherichia coli
More efficient protein targeting requires heterodimerization and activation of the GTPases present in the SRP receptor FtsY and the SRP protein Ffh. FtsY also forms a homodimer at the membrane using the same interaction surface as the heterodimer. Homodimerization adds to the complex interaction landscape of protein targeting. Biochemical analysis and integrative modeling suggest that the homodimer employs the same interface as the heterodimer. Ffh does not homodimerize while FtsY is able to form a homodimer. FtsY homodimer and FtsY/Ffh heterodimer share a similar interface Escherichia coli

Synonyms

Synonyms Comment Organism
FtsY GTPase
-
 Escherichia coli
SRP GTPase
-
 Escherichia coli
SRP receptor
-
 Escherichia coli

General Information

General Information Comment Organism
malfunction asymmetries in the catalytic center affect GTP hydrolysis, overview Escherichia coli
additional information efficient protein targeting requires heterodimerization and activation of the GTPases present in the SRP receptor FtsY and the SRP protein Ffh. FtsY also forms a homodimer at the membrane, in vitro and in vivo, using the same interaction surface as the heterodimer. Homodimerization adds to the complex interaction landscape of protein targeting. SRP binding to the receptor occurs by heterodimerization of the highly conserved NG domains of Ffh and FtsY, respectively, resulting in the formation of the so-called targeting complex. A dimerization-induced conformational switch of the nucleotide gamma-phosphate is conserved in Escherichia coli, filling an important gap in SRP GTPase activation. Asymmetries in the catalytic center affect GTP hydrolysis Escherichia coli