› 6mlu

Electron Microscopy
4Å resolution

Cryo-EM structure of lipid droplet formation protein Seipin/BSCL2

Released:
DOI: 10.2210/pdb6mlu/pdb
PDB entry 6mlu coloured by chain, front view.
PDB entry 6mlu coloured by chain, side view.
PDB entry 6mlu coloured by chain, top view.
Source organism: Drosophila melanogaster
Primary publication:
Cryo-electron microscopy structure of the lipid droplet-formation protein seipin.
Sui X, Arlt H, Brock KP, Lai ZW, DiMaio F, Marks DS, Liao M, Farese RV, Walther TC
OpenAccess logo J Cell Biol 217 4080-4091 (2018)
PMID: 30327422
Related structures: EMD-9146

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194194 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Seipin Chains: A, B
Molecule details ›
Chains: A, B
Length: 382 amino acids
Theoretical weight: 43.96 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9V3X4 (Residues: 2-370; Coverage: 100%)
Gene names: CG9904, Seipin
Sequence domains: Putative adipose-regulatory protein (Seipin)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 4Å
Relevant EMDB volumes: EMD-9146
Expression system: Escherichia coli

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Citations

26 review citations

Enzymatic Noncovalent Synthesis.
He et al. (2020)
25 more

4 mentions without citation

Mechanisms of Non-Vesicular Exchange of Lipids at Membrane Contact Sites: Of Shuttles, Tunnels and, Funnels.
Egea PF. (2021)
3 more