› 1kkt

X-ray diffraction
2.2Å resolution

Structure of P. citrinum alpha 1,2-mannosidase reveals the basis for differences in specificity of the ER and Golgi Class I enzymes

Released:
DOI: 10.2210/pdb1kkt/pdb
PDB entry 1kkt coloured by chain, front view.
PDB entry 1kkt coloured by chain, side view.
PDB entry 1kkt coloured by chain, top view.
Source organism: Penicillium citrinum
Primary publication:
Structure of Penicillium citrinum alpha 1,2-mannosidase reveals the basis for differences in specificity of the endoplasmic reticulum and Golgi class I enzymes.
Lobsanov YD, Vallée F, Imberty A, Yoshida T, Yip P, Herscovics A, Howell PL
J Biol Chem 277 5620-30 (2002)
PMID: 11714724

Function and Biology Details

Reaction catalysed: 
(1a) Man(9)GlcNAc(2)-[protein] + H(2)O = Man(8)GlcNAc(2)-[protein] (isomer 8A(1,2,3)B(1,2)) + beta-D-mannopyranose
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152076 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Mannosyl-oligosaccharide alpha-1,2-mannosidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 511 amino acids
Theoretical weight: 56.63 KDa
Source organism: Penicillium citrinum
Expression system: Aspergillus oryzae
UniProt:
  • Canonical: P31723 (Residues: 1-511; Coverage: 100%)
Gene name: MSDC
Sequence domains: Glycosyl hydrolase family 47
Structure domains: Glycosyltransferase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, MAN
Carbohydrate polymer
1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 56.487Å b: 110.997Å c: 86.235Å
α: 90° β: 99.17° γ: 90°
R-values:
R R work R free
0.197 0.193 0.239
Expression system: Aspergillus oryzae

Quick links

Citations

6 review citations

Glycosidase mechanisms.
Vasella et al. (2002)
5 more

1 mention without citation

Modulation of activity by Arg407: structure of a fungal alpha-1,2-mannosidase in complex with a substrate analogue.
Lobsanov et al. (2008)