› 3vp7

X-ray diffraction
2.3Å resolution

Crystal structure of the beta-alpha repeated, autophagy-specific (BARA) domain of Vps30/Atg6

Released:
DOI: 10.2210/pdb3vp7/pdb
PDB entry 3vp7 coloured by chain, front view.
PDB entry 3vp7 coloured by chain, side view.
PDB entry 3vp7 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Structure of the novel C-terminal domain of vacuolar protein sorting 30/autophagy-related protein 6 and its specific role in autophagy.
Noda NN, Kobayashi T, Adachi W, Fujioka Y, Ohsumi Y, Inagaki F
OpenAccess logo J Biol Chem 287 16256-66 (2012)
PMID: 22437838

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-554310 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vacuolar protein sorting-associated protein 30 Chain: A
Molecule details ›
Chain: A
Length: 220 amino acids
Theoretical weight: 24.68 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: Q02948 (Residues: 320-539; Coverage: 40%)
Gene names: APG6, ATG6, LPH7, VPS30, VPT30, YPL120W
Sequence domains: Apg6 BARA domain
Structure domains: Autophagy protein 6/Beclin 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P41212
Unit cell:
a: 59.959Å b: 59.959Å c: 113.977Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.209 0.243
Expression system: Escherichia coli

Quick links

Citations

17 review citations

Autophagy and autophagy-related proteins in cancer.
Li et al. (2020)
16 more

3 mentions without citation

Post-translationally-modified structures in the autophagy machinery: an integrative perspective.
Popelka et al. (2015)
2 more