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 (Comment) | Organism |
---|---|
subcloned between the EcoRI and PstI sites of the expression vector pKK223-3, expression in Escherichia coli strain JM109 | Thermus caldophilus |
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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Thermus caldophilus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermus caldophilus | Q08GC7 | - |
- |
Purification (Comment) | Organism |
---|---|
by heat treatment, ion exchange chromatography, and gel filtration | Thermus caldophilus |
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 | Comment | Organism |
---|---|---|
PGK | - |
Thermus caldophilus |