1BU6

CRYSTAL STRUCTURES OF ESCHERICHIA COLI GLYCEROL KINASE AND THE MUTANT A65T IN AN INACTIVE TETRAMER: CONFORMATIONAL CHANGES AND IMPLICATIONS FOR ALLOSTERIC REGULATION

Summary for 1BU6

• Entry DOI: 10.2210/pdb1bu6/pdb
• Descriptor: PROTEIN (GLYCEROL KINASE), SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: allostery, cooperativity, glycerol kinase, transferase
• Biological source: Escherichia coli
• Total number of polymer chains: 4
• Total formula weight: 225714.27

Authors

Feese, M.D.,Faber, H.R.,Bystrom, C.E.,Pettigrew, D.W.,Remington, S.J. (deposition date: 1998-08-30, release date: 1998-09-16, Last modification date: 2023-08-09)

Primary citation

Feese, M.D.,Faber, H.R.,Bystrom, C.E.,Pettigrew, D.W.,Remington, S.J.
Glycerol kinase from Escherichia coli and an Ala65-->Thr mutant: the crystal structures reveal conformational changes with implications for allosteric regulation.
Structure, 6:1407-1418, 1998

PubMed 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.

PubMed: 9817843
DOI: 10.1016/S0969-2126(98)00140-3

Experimental method

X-RAY DIFFRACTION (2.37 Å)