› 3a7p

X-ray diffraction
2.8Å resolution

The crystal structure of Saccharomyces cerevisiae Atg16

Released:
DOI: 10.2210/pdb3a7p/pdb
PDB entry 3a7p coloured by chain, front view.
PDB entry 3a7p coloured by chain, side view.
PDB entry 3a7p coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Dimeric coiled-coil structure of Saccharomyces cerevisiae Atg16 and its functional significance in autophagy.
Fujioka Y, Noda NN, Nakatogawa H, Ohsumi Y, Inagaki F
J Biol Chem 285 1508-15 (2010)
PMID: 19889643

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169949 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Autophagy protein 16 Chains: A, B
Molecule details ›
Chains: A, B
Length: 152 amino acids
Theoretical weight: 17.3 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q03818 (Residues: 1-150; Coverage: 100%)
Gene names: APG15, APG16, ATG16, CVT11, SAP18, YM8520.08C, YMR159C
Sequence domains: Autophagy protein 16 (ATG16)
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P6222
Unit cell:
a: 114.191Å b: 114.191Å c: 156.286Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.254 0.253 0.264
Expression system: Escherichia coli BL21

Quick links

Citations

37 review citations

The role of Atg proteins in autophagosome formation.
Mizushima et al. (2011)
36 more

6 mentions without citation

Challenges in homology search: HMMER3 and convergent evolution of coiled-coil regions.
Mistry et al. (2013)
5 more