› 3q2p

X-ray diffraction
2.34Å 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/pdb3q2p/pdb
PDB entry 3q2p coloured by chain, front view.
PDB entry 3q2p coloured by chain, side view.
PDB entry 3q2p 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:
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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 97 amino acids
Theoretical weight: 11.41 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

1 bound ligand:
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 31.4Å b: 144.1Å c: 45.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.184 0.245
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

1 mention 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)