› 6eoc

X-ray diffraction
1.67Å resolution

Crystal structure of AMPylated GRP78 in apo form (Crystal form 2)

Released:
DOI: 10.2210/pdb6eoc/pdb
PDB entry 6eoc coloured by chain, front view.
PDB entry 6eoc coloured by chain, side view.
PDB entry 6eoc coloured by chain, top view.
Source organism: Cricetulus griseus
Primary publication:
AMPylation targets the rate-limiting step of BiP's ATPase cycle for its functional inactivation.
Preissler S, Rohland L, Yan Y, Chen R, Read RJ, Ron D
Elife 6 (2017)
PMID: 29064368

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124345 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoplasmic reticulum chaperone BiP Chain: A
Molecule details ›
Chain: A
Length: 522 amino acids
Theoretical weight: 57.41 KDa
Source organism: Cricetulus griseus
Expression system: Escherichia coli
UniProt:
  • Canonical: G3I8R9 (Residues: 28-549; Coverage: 82%)
Gene names: GRP78, HSPA5, I79_019946
Sequence domains: Hsp70 protein
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand FLC 1 x FLC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: P212121
Unit cell:
a: 69.088Å b: 75.408Å c: 98.308Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.211 0.249
Expression system: Escherichia coli

Quick links

Citations

8 review citations

The endoplasmic reticulum (ER) chaperone BiP is a master regulator of ER functions: Getting by with a little help from ERdj friends.
Pobre et al. (2019)
7 more

2 mentions without citation

GRP78: A cell's response to stress.
Ibrahim et al. (2019)
1 more