› 1ymv

X-ray diffraction
1.9Å resolution

SIGNAL TRANSDUCTION PROTEIN CHEY MUTANT WITH PHE 14 REPLACED BY GLY, SER 15 REPLACED BY GLY, AND MET 17 REPLACED BY GLY

Released:
DOI: 10.2210/pdb1ymv/pdb
PDB entry 1ymv coloured by chain, front view.
PDB entry 1ymv coloured by chain, side view.
PDB entry 1ymv coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The three-dimensional structure of two mutants of the signal transduction protein CheY suggest its molecular activation mechanism.
Bellsolell L, Cronet P, Majolero M, Serrano L, Coll M
J Mol Biol 257 116-28 (1996)
PMID: 8632450

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142405 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chemotaxis protein CheY Chain: A
Molecule details ›
Chain: A
Length: 129 amino acids
Theoretical weight: 13.96 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AE67 (Residues: 2-129; Coverage: 99%)
Gene names: JW1871, b1882, cheY
Sequence domains: Response regulator receiver domain
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 37.1Å b: 53.9Å c: 57.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 not available
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Two-component signal transduction.
Stock et al. (2000)
2 more

1 mention without citation

Relating destabilizing regions to known functional sites in proteins.
Dessailly et al. (2007)