› 3olv

X-ray diffraction
1.7Å resolution

Structural and functional effects of substitution at position T+1 in CheY: CheYA88V-BeF3-Mg complex

Released:
DOI: 10.2210/pdb3olv/pdb
PDB entry 3olv coloured by chain, front view.
PDB entry 3olv coloured by chain, side view.
PDB entry 3olv 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: 14.14 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

3 bound ligands:
Ligand MG 2 x MG
Ligand BEF 6 x BEF
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P1
Unit cell:
a: 41.477Å b: 44.799Å c: 48.069Å
α: 69.23° β: 68.01° γ: 66.16°
R-values:
R R work R free
0.176 0.174 0.209
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)