› 1mol

X-ray diffraction
1.7Å resolution

TWO CRYSTAL STRUCTURES OF A POTENTLY SWEET PROTEIN: NATURAL MONELLIN AT 2.75 ANGSTROMS RESOLUTION AND SINGLE-CHAIN MONELLIN AT 1.7 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1mol/pdb
PDB entry 1mol coloured by chain, front view.
PDB entry 1mol coloured by chain, side view.
PDB entry 1mol coloured by chain, top view.
Source organism: Dioscoreophyllum cumminsii
Primary publication:
Two crystal structures of a potently sweet protein. Natural monellin at 2.75 A resolution and single-chain monellin at 1.7 A resolution.
Somoza JR, Jiang F, Tong L, Kang CH, Cho JM, Kim SH
J Mol Biol 234 390-404 (1993)
PMID: 8230222

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136329 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Monellin chain B Chains: A, B
Molecule details ›
Chains: A, B
Length: 94 amino acids
Theoretical weight: 11.08 KDa
Source organism: Dioscoreophyllum cumminsii
Expression system: Not provided
UniProt:
  • Canonical: P02882 (Residues: 1-42, 45-48; Coverage: 92%)
Sequence domains: Monellin
Structure domains: Nuclear Transport Factor 2; Chain: A,

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 46.36Å b: 49.09Å c: 40.72Å
α: 90° β: 102.86° γ: 90°
R-values:
R R work R free
0.174 0.174 not available
Expression system: Not provided

Quick links

Citations

4 review citations

Developments in biotechnological production of sweet proteins.
Masuda et al. (2006)
3 more

26 mentions without citation

Protein reconstitution and three-dimensional domain swapping: benefits and constraints of covalency.
Carey et al. (2007)
25 more