PMID:9817843
| Citation |
Feese, MD, Faber, HR, Bystrom, CE, Pettigrew, DW and Remington, SJ (1998) Glycerol kinase from Escherichia coli and an Ala65-->Thr mutant: the crystal structures reveal conformational changes with implications for allosteric regulation. Structure 6:1407-18 |
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| Abstract |
Glycerol kinase (GK) from Escherichia coli is a velocity-modulated (V system) enzyme that has three allosteric effectors with independent mechanisms: fructose-1,6-bisphosphate (FBP); the phosphocarrier protein IIAGlc; and adenosine nucleotides. The enzyme exists in solution as functional dimers that associate reversibly to form tetramers. GK is a member of a superfamily of ATPases that share a common ATPase domain and are thought to undergo a large conformational change as an intrinsic step in their catalytic cycle. Members of this family include actin, hexokinase and the heat shock protein hsc70. |
| Links | |
| Keywords |
Alanine/chemistry; Allosteric Regulation; Amino Acid Substitution; Binding Sites; Crystallography, X-Ray; Dimerization; Escherichia coli/enzymology; Glycerol Kinase/chemistry; Glycerol Kinase/metabolism; Protein Conformation; Threonine/chemistry |
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