› 2lvw

Solution NMR

Solution NMR studies of the dimeric regulatory subunit IlvN of the E.coli Acetohydroxyacid synthase I (AHAS I)

Released:
DOI: 10.2210/pdb2lvw/pdb
PDB entry 2lvw coloured by chain, ensemble of 20 models, front view.
PDB entry 2lvw coloured by chain, ensemble of 20 models, side view.
PDB entry 2lvw coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia coli K-12
Primary publication:
The coil-to-helix transition in IlvN regulates the allosteric control of Escherichia coli acetohydroxyacid synthase I.
Karanth NM, Sarma SP
Biochemistry 52 70-83 (2013)
PMID: 23205845

Function and Biology Details

Reaction catalysed: 
2 pyruvate = 2-acetolactate + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142354 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetolactate synthase isozyme 1 small subunit Chains: A, B
Molecule details ›
Chains: A, B
Length: 98 amino acids
Theoretical weight: 11.26 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ADF8 (Residues: 1-96; Coverage: 100%)
Gene names: JW3645, b3670, ilvN
Sequence domains: ACT domain
Structure domains: Alpha-Beta Plaits

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this NMR entry.
Chemical shift assignment: 42%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Allosteric ACTion: the varied ACT domains regulating enzymes of amino-acid metabolism.
Lang et al. (2014)
1 more

3 mentions without citation

Sequence co-evolution gives 3D contacts and structures of protein complexes.
Hopf et al. (2014)
2 more