› 1o7d

X-ray diffraction
2.7Å resolution

The structure of the bovine lysosomal a-mannosidase suggests a novel mechanism for low pH activation

Released:
DOI: 10.2210/pdb1o7d/pdb
PDB entry 1o7d coloured by chain, front view.
PDB entry 1o7d coloured by chain, side view.
PDB entry 1o7d coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
The structure of bovine lysosomal alpha-mannosidase suggests a novel mechanism for low-pH activation.
Heikinheimo P, Helland R, Leiros HK, Leiros I, Karlsen S, Evjen G, Ravelli R, Schoehn G, Ruigrok R, Tollersrud OK, McSweeney S, Hough E
J Mol Biol 327 631-44 (2003)
PMID: 12634058

Function and Biology Details

Reaction catalysed: 
Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173348 (preferred)
Entry contents:
5 distinct polypeptide molecules
Macromolecules (7 distinct):
Lysosomal alpha-mannosidase A peptide Chain: A
Molecule details ›
Chain: A
Length: 298 amino acids
Theoretical weight: 34.53 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: Q29451 (Residues: 51-348; Coverage: 31%)
Gene names: MAN2B1, MANB
Sequence domains: Glycosyl hydrolases family 38 N-terminal domain
Structure domains: Glycoside hydrolase 38, N terminal domain
Lysosomal alpha-mannosidase B peptide Chain: B
Molecule details ›
Chain: B
Length: 84 amino acids
Theoretical weight: 9.65 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: Q29451 (Residues: 349-432; Coverage: 9%)
Gene names: MAN2B1, MANB
Sequence domains: Alpha mannosidase middle domain
Structure domains: Glycoside hydrolase family 38, central domain
Lysosomal alpha-mannosidase C peptide Chain: C
Molecule details ›
Chain: C
Length: 159 amino acids
Theoretical weight: 17.6 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: Q29451 (Residues: 433-591; Coverage: 17%)
Gene names: MAN2B1, MANB
Sequence domains:
Structure domains:
Lysosomal alpha-mannosidase D peptide Chain: D
Molecule details ›
Chain: D
Length: 282 amino acids
Theoretical weight: 32.23 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: Q29451 (Residues: 592-873; Coverage: 30%)
Gene names: MAN2B1, MANB
Sequence domains: Glycosyl hydrolases family 38 C-terminal domain
Structure domains: Golgi alpha-mannosidase II; domain 4
Lysosomal alpha-mannosidase E peptide Chain: E
Molecule details ›
Chain: E
Length: 126 amino acids
Theoretical weight: 14.05 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: Q29451 (Residues: 874-999; Coverage: 13%)
Gene names: MAN2B1, MANB
Structure domains: Immunoglobulin-like

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
4 bound ligands:
Ligand NAG 1 x NAG
Ligand TRS 1 x TRS
Ligand ZN 1 x ZN
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P6122
Unit cell:
a: 117.88Å b: 117.88Å c: 582.04Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.257 0.257 0.289

Quick links

Citations

4 review citations

Why are proteins charged? Networks of charge-charge interactions in proteins measured by charge ladders and capillary electrophoresis.
Gitlin et al. (2006)
3 more

12 mentions without citation

The structure of bovine lysosomal alpha-mannosidase suggests a novel mechanism for low-pH activation.
Heikinheimo et al. (2003)
11 more