› 3vu1

X-ray diffraction
2.7Å resolution

Crystal structure of the C-terminal globular domain of oligosaccharyltransferase (PhAglB-L, O74088_PYRHO) from Pyrococcus horikoshii

Released:
DOI: 10.2210/pdb3vu1/pdb
PDB entry 3vu1 coloured by chain, front view.
PDB entry 3vu1 coloured by chain, side view.
PDB entry 3vu1 coloured by chain, top view.
Source organism: Pyrococcus horikoshii OT3
Primary publication:
Crystallographic and NMR evidence for flexibility in oligosaccharyltransferases and its catalytic significance.
Nyirenda J, Matsumoto S, Saitoh T, Maita N, Noda NN, Inagaki F, Kohda D
Structure 21 32-41 (2013)
PMID: 23177926

Function and Biology Details

Reaction catalysed: 
An archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-130770 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dolichyl-phosphooligosaccharide-protein glycotransferase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 506 amino acids
Theoretical weight: 57.56 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
  • Canonical: O74088 (Residues: 482-976; Coverage: 51%)
Gene names: PH0242, aglB1
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CA 2 x CA
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P212121
Unit cell:
a: 83.467Å b: 94.844Å c: 186.345Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.171 0.215
Expression system: Escherichia coli

Quick links

Citations

3 review citations

N-linked glycosylation in Archaea: a structural, functional, and genetic analysis.
Jarrell et al. (2014)
2 more

1 mention without citation

Structural Insight into the Mechanism of N-Linked Glycosylation by Oligosaccharyltransferase.
Mohanty et al. (2020)