› 1n7g

X-ray diffraction
2.2Å resolution

Crystal Structure of the GDP-mannose 4,6-dehydratase ternary complex with NADPH and GDP-rhamnose.

Released:
DOI: 10.2210/pdb1n7g/pdb
PDB entry 1n7g coloured by chain, front view.
PDB entry 1n7g coloured by chain, side view.
PDB entry 1n7g coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Structure of the MUR1 GDP-mannose 4,6-dehydratase from Arabidopsis thaliana: implications for ligand binding and specificity.
Mulichak AM, Bonin CP, Reiter WD, Garavito RM
Biochemistry 41 15578-89 (2002)
PMID: 12501186

Function and Biology Details

Reaction catalysed: 
GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161068 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GDP-mannose 4,6 dehydratase 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 381 amino acids
Theoretical weight: 43.08 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P93031 (Residues: 1-373; Coverage: 100%)
Gene names: At3g51160, F24M12.200, GMD2, MUR1
Sequence domains: GDP-mannose 4,6 dehydratase
Structure domains:

Ligands and Environments


Cofactor: Ligand NDP 4 x NDP
1 bound ligand:
Ligand GDR 3 x GDR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 5ID-B
Spacegroup: P212121
Unit cell:
a: 113.18Å b: 119.01Å c: 118.89Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.201 0.247
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

Medium- and short-chain dehydrogenase/reductase gene and protein families : the SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymes.
Kavanagh et al. (2008)
1 more

5 mentions without citation

Insight into S-adenosylmethionine biosynthesis from the crystal structures of the human methionine adenosyltransferase catalytic and regulatory subunits.
Shafqat et al. (2013)
4 more