› 4loc

X-ray diffraction
2.26Å resolution

Structure of the carboxyl transferase domain from Rhizobium etli pyruvate carboxylase with oxamate and biotin

Released:
DOI: 10.2210/pdb4loc/pdb
PDB entry 4loc coloured by chain, front view.
PDB entry 4loc coloured by chain, side view.
PDB entry 4loc coloured by chain, top view.
Source organism: Rhizobium etli CFN 42
Primary publication:
The role of biotin and oxamate in the carboxyltransferase reaction of pyruvate carboxylase.
Lietzan AD, Lin Y, St Maurice M
Arch Biochem Biophys 562 70-9 (2014)
PMID: 25157442

Function and Biology Details

Reaction catalysed: 
ATP + pyruvate + HCO(3)(-) = ADP + phosphate + oxaloacetate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173672 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate carboxylase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 632 amino acids
Theoretical weight: 69.96 KDa
Source organism: Rhizobium etli CFN 42
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q2K340 (Residues: 465-1067; Coverage: 52%)
Gene names: RHE_CH04002, pyc
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand BTN 4 x BTN
5 bound ligands:
Ligand ZN 4 x ZN
Ligand MG 4 x MG
Ligand CL 3 x CL
Ligand OXM 4 x OXM
Ligand GOL 2 x GOL
1 modified residue:
Ligand KCX 4 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P212121
Unit cell:
a: 83.87Å b: 157.123Å c: 244.714Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.176 0.216
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 citation in other articles

Comparative analysis of the Corynebacterium glutamicum transcriptome in response to changes in dissolved oxygen levels.
Liu et al. (2017)
3 more

1 mention without citation

The role of biotin and oxamate in the carboxyltransferase reaction of pyruvate carboxylase.
Lietzan et al. (2014)