› 1uux

X-ray diffraction
1.6Å resolution

Structure of a molybdopterin-bound cnx1g domain links molybdenum and copper metabolism

Released:
DOI: 10.2210/pdb1uux/pdb
PDB entry 1uux coloured by chain, front view.
PDB entry 1uux coloured by chain, side view.
PDB entry 1uux coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Structure of the molybdopterin-bound Cnx1G domain links molybdenum and copper metabolism.
Kuper J, Llamas A, Hecht HJ, Mendel RR, Schwarz G
Nature 430 803-6 (2004)
PMID: 15306815

Function and Biology Details

Reactions catalysed: 
Adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP
ATP + molybdopterin = diphosphate + adenylyl-molybdopterin
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174429 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Molybdopterin biosynthesis protein CNX1 Chain: A
Molecule details ›
Chain: A
Length: 163 amino acids
Theoretical weight: 17.2 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q39054 (Residues: 462-623; Coverage: 24%)
Gene names: At5g20990, CNX1, F22D1.6, T10F18.20
Sequence domains: Probable molybdopterin binding domain
Structure domains: MoaB/Mog-like domain

Ligands and Environments

5 bound ligands:
Ligand MTE 1 x MTE
Ligand PPI 1 x PPI
Ligand IMD 1 x IMD
Ligand FMT 1 x FMT
Ligand CU1 1 x CU1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: F4132
Unit cell:
a: 171.034Å b: 171.034Å c: 171.034Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.164 0.191
Expression system: Escherichia coli

Quick links

Citations

35 review citations

How do bacterial cells ensure that metalloproteins get the correct metal?
Waldron et al. (2009)
34 more

2 mentions without citation

Bacterial over-expression and purification of the 3'phosphoadenosine 5'phosphosulfate (PAPS) reductase domain of human FAD synthase: functional characterization and homology modeling.
Miccolis et al. (2012)
1 more