› 1glf

X-ray diffraction
2.62Å resolution

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

Released:
DOI: 10.2210/pdb1glf/pdb
PDB entry 1glf coloured by chain, front view.
PDB entry 1glf coloured by chain, side view.
PDB entry 1glf coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Glycerol kinase from Escherichia coli and an Ala65-->Thr mutant: the crystal structures reveal conformational changes with implications for allosteric regulation.
Feese MD, Faber HR, Bystrom CE, Pettigrew DW, Remington SJ
Structure 6 1407-18 (1998)
PMID: 9817843

Function and Biology Details

Reaction catalysed: 
ATP + glycerol = ADP + sn-glycerol 3-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141311 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycerol kinase Chains: O, X, Y, Z
Molecule details ›
Chains: O, X, Y, Z
Length: 501 amino acids
Theoretical weight: 56.16 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6F3 (Residues: 2-502; Coverage: 100%)
Gene names: JW3897, b3926, glpK
Sequence domains:
Structure domains: Nucleotidyltransferase; domain 5

Ligands and Environments

3 bound ligands:
Ligand PO4 2 x PO4
Ligand ADP 4 x ADP
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 92.1Å b: 117.4Å c: 108.4Å
α: 90° β: 93.1° γ: 90°
R-values:
R R work R free
0.146 0.146 not available
Expression system: Escherichia coli

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Citations

1 review citation

Dynamic dissociating homo-oligomers and the control of protein function.
Selwood et al. (2012)
26 other articles

6 mentions without citation

Mechanisms of selectivity in channels and enzymes studied with interactive molecular dynamics.
Grayson et al. (2003)
5 more