› 1xko

X-ray diffraction
2.48Å resolution

Structure of Thermotoga maritima CheX

Released:
DOI: 10.2210/pdb1xko/pdb
PDB entry 1xko coloured by chain, front view.
PDB entry 1xko coloured by chain, side view.
PDB entry 1xko coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Structure and function of an unusual family of protein phosphatases: the bacterial chemotaxis proteins CheC and CheX.
Park SY, Chao X, Gonzalez-Bonet G, Beel BD, Bilwes AM, Crane BR
Mol Cell 16 563-74 (2004)
PMID: 15546616

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194838 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CheY-P phosphatase CheX Chains: A, B
Molecule details ›
Chains: A, B
Length: 159 amino acids
Theoretical weight: 16.88 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9X1V3 (Residues: 1-155; Coverage: 100%)
Gene names: TM_1618, cheX
Sequence domains: CheC-like family
Structure domains: CheC-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P212121
Unit cell:
a: 52.21Å b: 67.9Å c: 78.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.24 0.295
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Molecular Mechanisms of Two-Component Signal Transduction.
Zschiedrich et al. (2016)
4 more

2 mentions without citation

Identical phosphatase mechanisms achieved through distinct modes of binding phosphoprotein substrate.
Pazy et al. (2010)
1 more