› 4frq

X-ray diffraction
2.35Å resolution

Crystal Structure of BBBB+UDP+Gal at pH 9.5 with MPD as the cryoprotectant

Released:
DOI: 10.2210/pdb4frq/pdb
PDB entry 4frq coloured by chain, front view.
PDB entry 4frq coloured by chain, side view.
PDB entry 4frq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
pH-induced conformational changes in human ABO(H) blood group glycosyltransferases confirm the importance of electrostatic interactions in the formation of the semi-closed state.
Johal AR, Blackler RJ, Alfaro JA, Schuman B, Borisova S, Evans SV
Glycobiology 24 237-46 (2014)
PMID: 24265507

Function and Biology Details

Reactions catalysed: 
UDP-alpha-D-galactose + alpha-L-fucosyl-(1->2)-D-galactosyl-R = UDP + alpha-D-galactosyl-(1->3)-(alpha-L-fucosyl-(1->2))-D-galactosyl-R
UDP-N-acetyl-alpha-beta-D-galactosamine + glycoprotein-alpha-L-fucosyl-(1->2)-D-galactose = UDP + glycoprotein-N-acetyl-alpha-D-galactosaminyl-(1->3)-(alpha-L-fucosyl-(1->2))-beta-D-galactose
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147726 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form Chain: A
Molecule details ›
Chain: A
Length: 293 amino acids
Theoretical weight: 34.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P16442 (Residues: 64-354; Coverage: 82%)
Gene name: ABO
Sequence domains: Glycosyltransferase family 6
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

4 bound ligands:
Ligand UDP 1 x UDP
Ligand PEG 1 x PEG
Ligand MN 1 x MN
Ligand GAL 1 x GAL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: C2221
Unit cell:
a: 52.307Å b: 151.386Å c: 79.397Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.182 0.252
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

High Resolution Structures of the Human ABO(H) Blood Group Enzymes in Complex with Donor Analogs Reveal That the Enzymes Utilize Multiple Donor Conformations to Bind Substrates in a Stepwise Manner.
Gagnon et al. (2015)
2 more