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Literature summary for 2.7.2.3 extracted from

  • Lee, J.H.; Im, Y.J.; Bae, J.; Kim, D.; Kim, M.K.; Kang, G.B.; Lee, D.S.; Eom, S.H.
    Crystal structure of Thermus caldophilus phosphoglycerate kinase in the open conformation (2006), Biochem. Biophys. Res. Commun., 350, 1044-1049.
    View publication on PubMed

Application

Application Comment Organism
additional information Arg148 as a key residue involved in open-to-closed transition, during catalysis, a conformational change occurs that brings the N- and C-domains of PGK closer together Thermus caldophilus

Cloned(Commentary)

Cloned (Comment) Organism
subcloned between the EcoRI and PstI sites of the expression vector pKK223-3, expression in Escherichia coli strain JM109 Thermus caldophilus

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of unliganded PGK, solved by molecular replacement to 1.8 A resolution, crystals belong to the P212121 space group with one molecule per asymmetric unit Thermus caldophilus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Thermus caldophilus

Organism

Organism UniProt Comment Textmining
Thermus caldophilus Q08GC7
-
-

Purification (Commentary)

Purification (Comment) Organism
by heat treatment, ion exchange chromatography, and gel filtration Thermus caldophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + 3-phospho-D-glyceroyl phosphate binding of 3-phospho-D-glycerate (or maybe 1,3-diphosphoglycerate) disrupts salt bridge between Arg148 and Glu375 and enables the formation of a new interdomain salt bridge between Arg60 and Asp197, which stabilizes the closed conformation Thermus caldophilus ATP + 3-phospho-D-glycerate
-
r

Synonyms

Synonyms Comment Organism
PGK
-
Thermus caldophilus