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Literature summary for 3.6.5.4 extracted from

  • Faoro, C.; Ataide, S.
    Structural insights into the G-loop dynamics of E. coli FtsY NG domain (2019), J. Struct. Biol., 208, 107387 .
    View publication on PubMed
Search for more literature for 3.6.5.4

Cloned(Commentary)

Cloned (Comment) Organism
genes ftsY and ffh, sequence comparisons Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant isolated FtsYNG domain in the nucleotide-free (apo) form, the GDP-bound, and the non-hydrolysable GTP-bound form (including GMPPNP (5'-guanylyl imidodiphosphate) and GMPPCP (beta,gamma-methyleneguanosine 5'-triphosphate)), X-ray diffraction structure determination and analysis at 1.22-1.88 A resolution Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, role of a magnesium ion during the GDP and GTP-bound states, overview. The binding of magnesium in the nucleotide site causes the reorientation of the beta-and gamma-phosphate groups toward the jaws of the P-loop and stabilizes the binding of the nucleotide, creating a network of hydrogen and water-bridge interactions 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 comparison of the nucleotide-free and GTP-bound structures of FtsY, catalytic mechanism and role of Mg2+, detailed overview Escherichia coli ?
-
-

Synonyms

Synonyms Comment Organism
FtsY
-
 Escherichia coli
signal recognition particle receptor
-
 Escherichia coli
SRP GTPase
-
 Escherichia coli
SRP receptor
-
 Escherichia coli

General Information

General Information Comment Organism
additional information analysis of the G-loop dynamics of FtsY NG domain, overview. The combination of high-resolution and multiple solved structures of FtsYNG in different states reveals a distinct sensor-relay system of the unique GTPase receptor. A nucleotide sensing function of the P-loop assists FtsYNG in nucleotide-binding and contributes to modulate nucleotide binding properties in SRP GTPases. A reorganization of the other G-loops and the insertion binding domain (IBD) is observed only upon transition from a diphosphate to a triphosphate nucleotide. The binding of magnesium in the nucleotide site causes the reorientation of the beta-and gamma-phosphate groups toward the jaws of the P-loop and stabilizes the binding of the nucleotide, creating a network of hydrogen and water-bridge interactions. An alternative conformation of the P-loop senses nucleotide-binding, FtsY P-loops dynamics, mechanism, detailed overview Escherichia coli