› 6utq

X-ray diffraction
2.39Å resolution

LarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase in complex with cadmium

Released:
DOI: 10.2210/pdb6utq/pdb
PDB entry 6utq coloured by chain, front view.
PDB entry 6utq coloured by chain, side view.
PDB entry 6utq coloured by chain, top view.
Source organism: Lactiplantibacillus plantarum
Primary publication:
Crystallographic characterization of a tri-Asp metal-binding site at the three-fold symmetry axis of LarE.
Fellner M, Huizenga KG, Hausinger RP, Hu J
Sci Rep 10 5830 (2020)
PMID: 32242052

Function and Biology Details

Reaction catalysed: 
(1a) ATP + pyridinium-3,5-dicarboxylate mononucleotide = diphosphate + 5-carboxy-1-(5-O-phospho-beta-D-ribofuranosyl)pyridinium-3-carbonyl adenylate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123801 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyridinium-3,5-bisthiocarboxylic acid mononucleotide synthase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 286 amino acids
Theoretical weight: 31.72 KDa
Source organism: Lactiplantibacillus plantarum
Expression system: Escherichia coli
UniProt:
  • Canonical: F9UST4 (Residues: 1-276; Coverage: 100%)
Gene names: larE, lp_0109
Sequence domains: NAD synthase

Ligands and Environments

3 bound ligands:
Ligand CD 7 x CD
Ligand PO4 6 x PO4
Ligand SO4 7 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P4122
Unit cell:
a: 107.775Å b: 107.775Å c: 319.633Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.213 0.254
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Comparison of insect and human cytochrome b561 proteins: Insights into candidate ferric reductases in insects.
Holst et al. (2023)

1 mention without citation

Crystallographic characterization of a tri-Asp metal-binding site at the three-fold symmetry axis of LarE.
Fellner et al. (2020)