Literature summary for 3.6.5.6 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.

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
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
Mg2+	-	Methanocaldococcus jannaschii
Na+	Na+ destabilizes the dimer and does not allow the positioning of the catalytic water molecule (molecular dynamics simulations)	Methanocaldococcus jannaschii

Organism

Organism	UniProt	Comment	Textmining
Methanocaldococcus jannaschii	Q57816	-	-

Subunits

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

Synonyms

Synonyms	Comment	Organism
FtsZ	-	Methanocaldococcus jannaschii

pH Stability

pH Stability	pH Stability Maximum	Comment	Organism
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

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Release 2023.1 (January 2023)