› 1bu6

X-ray diffraction
2.37Å 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/pdb1bu6/pdb
PDB entry 1bu6 coloured by chain, front view.
PDB entry 1bu6 coloured by chain, side view.
PDB entry 1bu6 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

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141309 (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: 56.19 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

2 bound ligands:
Ligand SO4 6 x SO4
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: 91.9Å b: 119Å c: 109.3Å
α: 90° β: 103.4° γ: 90°
R-values:
R R work R free
0.167 0.167 not available
Expression system: Escherichia coli

Quick links

Citations

1 review citation

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

5 mentions without citation

Protein-protein docking benchmark version 3.0.
Hwang et al. (2008)
4 more