› 6vz1

Electron Microscopy
3.2Å resolution

Cryo-EM structure of human diacylglycerol O-acyltransferase 1 complexed with acyl-CoA substrate

Released:
DOI: 10.2210/pdb6vz1/pdb
PDB entry 6vz1 coloured by chain, front view.
PDB entry 6vz1 coloured by chain, side view.
PDB entry 6vz1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure and catalytic mechanism of a human triacylglycerol-synthesis enzyme.
Sui X, Wang K, Gluchowski NL, Elliott SD, Liao M, Walther TC, Farese RV
Nature 581 323-328 (2020)
PMID: 32433611
Related structures: EMD-21481

Function and Biology Details

Reactions catalysed: 
Acyl-CoA + 1,2-diacylglycerol = CoA + triacylglycerol
Acyl-CoA + retinol = CoA + retinyl ester
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131166 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Diacylglycerol O-acyltransferase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 488 amino acids
Theoretical weight: 55.34 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: O75907 (Residues: 1-488; Coverage: 100%)
Gene names: AGRP1, DGAT, DGAT1
Sequence domains: MBOAT, membrane-bound O-acyltransferase family

Ligands and Environments

2 bound ligands:
Ligand 6OU 4 x 6OU
Ligand 3VV 2 x 3VV
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.2Å
Relevant EMDB volumes: EMD-21481
Expression system: Homo sapiens

Quick links

Citations

10 review citations

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

5 mentions without citation

A rising tide lifts all MBOATs: recent progress in structural and functional understanding of membrane bound O-acyltransferases.
Pierce et al. (2023)
4 more