› 1iuq

X-ray diffraction
1.55Å resolution

The 1.55 A Crystal Structure of Glycerol-3-Phosphate Acyltransferase

Released:
DOI: 10.2210/pdb1iuq/pdb
PDB entry 1iuq coloured by chain, front view.
PDB entry 1iuq coloured by chain, side view.
PDB entry 1iuq coloured by chain, top view.
Source organism: Cucurbita moschata
Primary publication:
Substrate recognition and selectivity of plant glycerol-3-phosphate acyltransferases (GPATs) from Cucurbita moscata and Spinacea oleracea.
Tamada T, Feese MD, Ferri SR, Kato Y, Yajima R, Toguri T, Kuroki R
Acta Crystallogr D Biol Crystallogr 60 13-21 (2004)
PMID: 14684887

Function and Biology Details

Reactions catalysed: 
Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate
Acyl-[acyl-carrier-protein] + sn-glycerol 3-phosphate = [acyl-carrier-protein] + 1-acyl-sn-glycerol 3-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145284 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycerol-3-phosphate acyltransferase ATS12, chloroplastic Chain: A
Molecule details ›
Chain: A
Length: 367 amino acids
Theoretical weight: 41.17 KDa
Source organism: Cucurbita moschata
Expression system: Escherichia coli
UniProt:
  • Canonical: P10349 (Residues: 98-462; Coverage: 79%)
Gene names: AT2, ATS1;2
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 5 x SO4
Ligand GOL 6 x GOL
1 modified residue:
Ligand MSE 7 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL40B2
Spacegroup: P212121
Unit cell:
a: 58.138Å b: 63.604Å c: 115.862Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.201 0.219
Expression system: Escherichia coli

Quick links

Citations

2 review citations

sn-Glycerol-3-phosphate acyltransferases in plants.
Chen et al. (2011)
1 more

9 mentions without citation

How lipid droplets "TAG" along: Glycerolipid synthetic enzymes and lipid storage.
Wang et al. (2017)
8 more