› 3pxm

X-ray diffraction
1.8Å resolution

Reduced sweetness of a monellin (MNEI) mutant results from increased protein flexibility and disruption of a distant poly-(L-proline) II helix

Released:
DOI: 10.2210/pdb3pxm/pdb
PDB entry 3pxm coloured by chain, front view.
PDB entry 3pxm coloured by chain, side view.
PDB entry 3pxm coloured by chain, top view.
Source organism: Dioscoreophyllum cumminsii
Primary publication:
Reduced sweetness of a monellin (MNEI) mutant results from increased protein flexibility and disruption of a distant poly-(L-proline) II helix.
Templeton CM, Ostovar pour S, Hobbs JR, Blanch EW, Munger SD, Conn GL
Chem Senses 36 425-34 (2011)
PMID: 21343241

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136325 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Monellin chain A; Monellin chain B Chains: A, B
Molecule details ›
Chains: A, B
Length: 97 amino acids
Theoretical weight: 11.39 KDa
Source organism: Dioscoreophyllum cumminsii
Expression system: Escherichia coli
UniProt:
  • Canonical: P02882 (Residues: 1-50; Coverage: 100%)
  • Canonical: P02881 (Residues: 2-45; Coverage: 98%)
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
X-ray source: RIGAKU
Spacegroup: P1
Unit cell:
a: 29.889Å b: 39.652Å c: 45.153Å
α: 84.9° β: 80.25° γ: 83.9°
R-values:
R R work R free
0.179 0.177 0.219
Expression system: Escherichia coli

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Citations

2 review citations

Calculation of Raman optical activity spectra for vibrational analysis.
Mutter et al. (2015)
1 more

2 mentions without citation

Reduced sweetness of a monellin (MNEI) mutant results from increased protein flexibility and disruption of a distant poly-(L-proline) II helix.
Templeton et al. (2011)
1 more