› 5vni

X-ray diffraction
2.79Å resolution

Crystal structure of Sec23a/Sec24a/Sec22 complexed with a C-terminal FA sorting motif

Released:
DOI: 10.2210/pdb5vni/pdb
PDB entry 5vni coloured by chain, front view.
PDB entry 5vni coloured by chain, side view.
PDB entry 5vni coloured by chain, top view.
Source organisms:
Primary publication:
ER retention is imposed by COPII protein sorting and attenuated by 4-phenylbutyrate.
Ma W, Goldberg E, Goldberg J
Elife 6 (2017)
PMID: 28594326

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-126630 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Protein transport protein Sec23A Chain: A
Molecule details ›
Chain: A
Length: 764 amino acids
Theoretical weight: 86.18 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q15436 (Residues: 1-764; Coverage: 100%)
Gene name: SEC23A
Sequence domains:
Structure domains:
Protein transport protein Sec24A Chain: B
Molecule details ›
Chain: B
Length: 748 amino acids
Theoretical weight: 84.34 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: O95486 (Residues: 346-1093; Coverage: 68%)
Gene name: SEC24A
Sequence domains:
Structure domains:
Vesicle-trafficking protein SEC22b Chain: C
Molecule details ›
Chain: C
Length: 157 amino acids
Theoretical weight: 18.03 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: O08547 (Residues: 1-157; Coverage: 73%)
Gene names: Sec22b, Sec22l1
Sequence domains:
Structure domains: Longin domain
C-terminal FA Chain: D
Molecule details ›
Chain: D
Length: 5 amino acids
Theoretical weight: 524 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: C2
Unit cell:
a: 147.606Å b: 96.065Å c: 129.998Å
α: 90° β: 90.06° γ: 90°
R-values:
R R work R free
0.215 0.212 0.27
Expression systems:
  • Trichoplusia ni
  • Escherichia coli
  • Not provided

Quick links

Citations

12 review citations

Pharmacological targeting of endoplasmic reticulum stress in disease.
Marciniak et al. (2022)
11 more

1 mention without citation

ER retention is imposed by COPII protein sorting and attenuated by 4-phenylbutyrate.
Ma et al. (2017)