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Literature summary extracted from

  • Mendieta, J.; Rico, A.I.; Lopez-Vinas, E.; Vicente, M.; Mingorance, J.; Gomez-Puertas, P.
    Structural and functional model for ionic (K(+)/Na(+)) and pH dependence of GTPase activity and polymerization of FtsZ, the prokaryotic ortholog of tubulin (2009), J. Mol. Biol., 390, 17-25.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.5.6 K+ K+ ion at the GTP binding site allows the positioning of one water molecule that interacts with catalytic residues D235 and D238, K+ ion stabilizes dimer (molecular dynamics simulations) Methanocaldococcus jannaschii
3.6.5.6 Mg2+
-
 Methanocaldococcus jannaschii
3.6.5.6 Na+ Na+ destabilizes the dimer and does not allow the positioning of the catalytic water molecule (molecular dynamics simulations) Methanocaldococcus jannaschii

Organism

EC Number Organism UniProt Comment Textmining
3.6.5.6 Methanocaldococcus jannaschii Q57816
-
-

Subunits

EC Number Subunits Comment Organism
3.6.5.6 More can polimerize in vitro, analysis of the dimer Methanocaldococcus jannaschii

Synonyms

EC Number Synonyms Comment Organism
3.6.5.6 FtsZ
-
 Methanocaldococcus jannaschii

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.6.5.6 additional information
-
 protonation of the GTP gamma-phosphate, simulating low pH, excludes both monovalent cations and the catalytic water molecule from the GTP binding site and stabilizes the dimer Methanocaldococcus jannaschii