› 1on8

X-ray diffraction
2.7Å resolution

Crystal structure of mouse alpha-1,4-N-acetylhexosaminyltransferase (EXTL2) with UDP and GlcUAb(1-3)Galb(1-O)-naphthalenelmethanol an acceptor substrate analog

Released:
DOI: 10.2210/pdb1on8/pdb
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PDB entry 1on8 coloured by chain, front view.
PDB entry 1on8 coloured by chain, side view.
PDB entry 1on8 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Crystal structure of an alpha 1,4-N-acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis.
Pedersen LC, Dong J, Taniguchi F, Kitagawa H, Krahn JM, Pedersen LG, Sugahara K, Negishi M
J Biol Chem 278 14420-8 (2003)
PMID: 12562774

Function and Biology Details

Reaction catalysed: 
UDP-N-acetyl-alpha-D-glucosamine + [protein]-3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-serine = UDP + [protein]-3-O-(alpha-D-GlcNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-serine
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo octamer
Assembly name:
PDBe Complex ID:
PDB-CPX-190190 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Exostosin-like 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 293 amino acids
Theoretical weight: 33.4 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9ES89 (Residues: 38-330; Coverage: 89%)
Gene names: Extl2, Extr2
Sequence domains: Glycosyl transferase family 64 domain
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

Carbohydrate polymer : NEW Components: GAL, BDP
Carbohydrate polymer
3 bound ligands:
Ligand MN 2 x MN
Ligand UDP 2 x UDP
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU RU300
Spacegroup: P4212
Unit cell:
a: 125.157Å b: 125.157Å c: 83.692Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.192 0.254
Expression system: Escherichia coli BL21(DE3)

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Citations

14 review citations

Glycosyltransferases: structures, functions, and mechanisms.
Lairson et al. (2008)
13 more

7 mentions without citation

Emerging structural insights into glycosyltransferase-mediated synthesis of glycans.
Moremen et al. (2019)
6 more

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