Conformational dynamics in phosphoglycerate kinase, an open and shut case?

• Published in: FEBS letters Vol. 587; no. 13; pp. 1878 - 1883
• Main Author: Bowler, Matthew W.
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 27.06.2013
• Subjects: 1,3BPG; 3-phosphoglycerate; 3PG; adenosine triphosphate; bisphosphoglycerate; carcinogenesis; catalytic activity; Catalytic Domain; crystal structure; Enzyme mechanism; glycolysis; hPGK; human phosphoglycerate kinase; Humans; Models, Molecular; phosphoglycerate kinase; Phosphoglycerate Kinase - chemistry; Phosphoryl transfer; Phosphorylation; Protein Structure, Secondary; Retroviridae; SAXS; Surface Properties; X-ray diffraction; 1,3BPG; 3PG; Enzyme mechanism; hPGK; Phosphoryl transfer; SAXS
• ISSN: 0014-5793; 1873-3468; 1873-3468
• DOI: 10.1016/j.febslet.2013.05.012

Domain motions are essential to many catalytic mechanisms in enzymes but they are often difficult to study. X-ray crystal structures can provide molecular details of snapshots of catalysis but many states important in the cycle remain inaccessible using this technique. Phosphoglycerate kinase (PGK)...