Literature summary for 4.1.1.85 extracted from

Li, G.L.; Liu, X.; Nan, J.; Brostromer, E.; Li, L.F.; Su, X.D.
Open-closed conformational change revealed by the crystal structures of 3-keto-L-gulonate 6-phosphate decarboxylase from Streptococcus mutans (2009), Biochem. Biophys. Res. Commun., 381, 429-433.

Cloned(Commentary)

Cloned (Comment)	Organism
into pET-28a vector containing an N-terminal His6-tag and expressed in Escherichia coli strain BL21 (DE3) cells	Streptococcus mutans

Crystallization (Commentary)

Crystallization (Comment)	Organism
at 289 K using the hanging-drop vapor-diffusion technique. Apoenzyme obtained in two different space groups P212121 (without Mg2+) and I422 (in complex with Mg2+) and in the absence and presence of the product analog D-ribulose 5-phosphate. An 8 A alphaB-helix movement and other structural rearrangements around the active site between the apostructures and product analog bound structure. Conformational flexibility around the active site for substrate/product binding. Especially the alphaB-helix (residues 144-149) and the side chains of the conserved Arg144 and Arg197 exhibit openclosed conformational changes between the apo-structure and complex structure with ligand bound at the active site	Streptococcus mutans

Crystallization (Comment)

Organism

at 289 K using the hanging-drop vapor-diffusion technique. Apoenzyme obtained in two different space groups P212121 (without Mg2+) and I422 (in complex with Mg2+) and in the absence and presence of the product analog D-ribulose 5-phosphate. An 8 A alphaB-helix movement and other structural rearrangements around the active site between the apostructures and product analog bound structure. Conformational flexibility around the active site for substrate/product binding. Especially the alphaB-helix (residues 144-149) and the side chains of the conserved Arg144 and Arg197 exhibit openclosed conformational changes between the apo-structure and complex structure with ligand bound at the active site

Streptococcus mutans

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	Mg2+ dependent decarboxylation	Streptococcus mutans

Organism

Organism	UniProt	Comment	Textmining
Streptococcus mutans	-	-	-
Streptococcus mutans UA159	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
on Ni2+-chelating affinity column and by gel filtration	Streptococcus mutans

Subunits

Subunits	Comment	Organism
homodimer	gel filtration	Streptococcus mutans

Synonyms

Synonyms	Comment	Organism
3-keto-L-gulonate 6-phosphate decarboxylase	-	Streptococcus mutans
KGPDC	-	Streptococcus mutans