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Literature summary for 2.7.2.3 extracted from

  • Marston, J.P.; Cliff, M.J.; Reed, M.A.; Blackburn, G.M.; Hounslow, A.M.; Craven, C.J.; Waltho, J.P.
    Structural tightening and interdomain communication in the catalytic cycle of phosphoglycerate kinase (2010), J. Mol. Biol., 396, 345-360.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
mutant W290Y Geobacillus stearothermophilus

Protein Variants

Protein Variants Comment Organism
W290Y has a negligible effect on its catalytic activity but improves protein solubility Geobacillus stearothermophilus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Geobacillus stearothermophilus

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus P18912
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-

Purification (Commentary)

Purification (Comment) Organism
mutant W290Y Geobacillus stearothermophilus

Storage Stability

Storage Stability Organism
4°C, 80% saturated ammonium sulfate solution Geobacillus stearothermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + 3-phospho-D-glyceroyl 1-phosphate overall increases in amide protection from hydrogen exchange when the W290Y mutant protein binds the substrate and product ligands and an additional increase when the transition-state analogue complex containing a 3-phospho-D-glycerate-(AlF4-)-ADP moiety is formed. Communication between domains is manifested in the accessibility of higher-energy, exchange-competent states. For residue D33, chemical shifts only change significantly upon transition-state analogue binding. For residue S346, chemical shifts change significantly upon ADP and transition-state analogue binding. For residue S58, chemical shifts are affected by 3-phospho-D-glycerate and transition-state analogue binding Geobacillus stearothermophilus ATP + 3-phospho-D-glycerate
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Synonyms

Synonyms Comment Organism
PGK
-
Geobacillus stearothermophilus
phosphoglycerate kinase
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Geobacillus stearothermophilus