› 5kym

X-ray diffraction
2.8Å resolution

Crystal Structure of the 1-acyl-sn-glycerophosphate (LPA) acyltransferase, PlsC, from Thermotoga maritima

Released:
DOI: 10.2210/pdb5kym/pdb
PDB entry 5kym coloured by chain, front view.
PDB entry 5kym coloured by chain, side view.
PDB entry 5kym coloured by chain, top view.
Source organism: Thermotoga maritima MSB8
Primary publication:
A two-helix motif positions the lysophosphatidic acid acyltransferase active site for catalysis within the membrane bilayer.
Robertson RM, Yao J, Gajewski S, Kumar G, Martin EW, Rock CO, White SW
Nat Struct Mol Biol 24 666-671 (2017)
PMID: 28714993

Function and Biology Details

Reaction catalysed: 
Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194856 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
1-acyl-sn-glycerol-3-phosphate acyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 247 amino acids
Theoretical weight: 28.74 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9X219 (Residues: 1-247; Coverage: 100%)
Gene name: TM_1693
Sequence domains: Acyltransferase

Ligands and Environments

3 bound ligands:
Ligand HGX 6 x HGX
Ligand DD9 2 x DD9
Ligand LMT 1 x LMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: I23
Unit cell:
a: 173.836Å b: 173.836Å c: 173.836Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.219 0.277
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

The Structure and Function of Acylglycerophosphate Acyltransferase 4/ Lysophosphatidic Acid Acyltransferase Delta (AGPAT4/LPAATδ).
Zhukovsky et al. (2019)
3 more

12 mentions without citation

Update and nomenclature proposal for mammalian lysophospholipid acyltransferases, which create membrane phospholipid diversity.
Valentine et al. (2022)
11 more