› 3oly

X-ray diffraction
2.05Å resolution

Structural and functional effects of substitution at position T+1 in CheY: CheYA88M-BeF3-Mn complex

Released:
DOI: 10.2210/pdb3oly/pdb
PDB entry 3oly coloured by chain, front view.
PDB entry 3oly coloured by chain, side view.
PDB entry 3oly coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
A Variable Active Site Residue Influences the Kinetics of Response Regulator Phosphorylation and Dephosphorylation.
Immormino RM, Silversmith RE, Bourret RB
Biochemistry 55 5595-5609 (2016)
PMID: 27589219

Function and Biology Details

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

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 129 amino acids
Theoretical weight: 14.17 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AE67 (Residues: 1-129; Coverage: 100%)
Gene names: JW1871, b1882, cheY
Sequence domains: Response regulator receiver domain
Structure domains: Rossmann fold

Ligands and Environments

4 bound ligands:
Ligand BEF 2 x BEF
Ligand MN 6 x MN
Ligand GOL 5 x GOL
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P212121
Unit cell:
a: 53.445Å b: 53.547Å c: 161.082Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.18 0.212
Expression system: Escherichia coli

Quick links

Citations

1 review citation

General strategies for using amino acid sequence data to guide biochemical investigation of protein function.
Kennedy et al. (2022)
8 other articles

1 mention without citation

A Variable Active Site Residue Influences the Kinetics of Response Regulator Phosphorylation and Dephosphorylation.
Immormino et al. (2016)