› 2gn1

X-ray diffraction
2.2Å resolution

Crystal structure of dimeric biodegradative threonine deaminase (TdcB) from Salmonella typhimurium at 2.2A resolution (Triclinic form with one dimer of TdcB in the asymmetric unit)

Released:
DOI: 10.2210/pdb2gn1/pdb
PDB entry 2gn1 coloured by chain, front view.
PDB entry 2gn1 coloured by chain, side view.
PDB entry 2gn1 coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Primary publication:
Crystal structures of Salmonella typhimurium biodegradative threonine deaminase and its complex with CMP provide structural insights into ligand-induced oligomerization and enzyme activation.
Simanshu DK, Savithri HS, Murthy MR
J Biol Chem 281 39630-41 (2006)
PMID: 17046821

Function and Biology Details

Reactions catalysed: 
(1a) L-serine = 2-aminoprop-2-enoate + H(2)O
(1a) L-threonine = 2-aminobut-2-enoate + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146008 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-threonine dehydratase catabolic TdcB Chains: A, B
Molecule details ›
Chains: A, B
Length: 342 amino acids
Theoretical weight: 36.89 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli
UniProt:
  • Canonical: P11954 (Residues: 2-329; Coverage: 100%)
Gene names: STM3244, tdcB
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand NA 1 x NA
1 modified residue:
Ligand LLP 2 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P1
Unit cell:
a: 46.317Å b: 55.3Å c: 67.235Å
α: 103.09° β: 94.7° γ: 112.94°
R-values:
R R work R free
0.212 0.21 0.253
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Structure and function of enzymes involved in the anaerobic degradation of L-threonine to propionate.
Simanshu et al. (2007)
21 other articles

1 mention without citation

Crystal structure of Escherichia coli diaminopropionate ammonia-lyase reveals mechanism of enzyme activation and catalysis.
Bisht et al. (2012)