› 1rm0

X-ray diffraction
2.05Å resolution

Crystal Structure of Myo-Inositol 1-Phosphate Synthase From Saccharomyces cerevisiae In Complex With NAD+ and 2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate

Released:
DOI: 10.2210/pdb1rm0/pdb
PDB entry 1rm0 coloured by chain, front view.
PDB entry 1rm0 coloured by chain, side view.
PDB entry 1rm0 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
The structure of the 1L-myo-inositol-1-phosphate synthase-NAD+-2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate complex demands a revision of the enzyme mechanism.
Jin X, Foley KM, Geiger JH
J Biol Chem 279 13889-95 (2004)
PMID: 14684747

Function and Biology Details

Reaction catalysed: 
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146022 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Inositol-3-phosphate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 533 amino acids
Theoretical weight: 59.71 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P11986 (Residues: 1-533; Coverage: 100%)
Gene names: INO1, J0610, YJL153C
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAI 2 x NAI
2 bound ligands:
Ligand MN 1 x MN
Ligand D6P 1 x D6P
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: C2
Unit cell:
a: 151.81Å b: 97.78Å c: 122.29Å
α: 90° β: 126.3° γ: 90°
R-values:
R R work R free
0.21 0.189 0.244
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Transient oxidation as a mechanistic strategy in enzymatic catalysis.
Tanner ME. (2008)
7 other articles

2 mentions without citation

An evolutionary analysis identifies a conserved pentapeptide stretch containing the two essential lysine residues for rice L-myo-inositol 1-phosphate synthase catalytic activity.
Basak et al. (2017)
1 more