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Structure paper

TitleUnravelling the amyloid aggregation mechanism of the sweet protein Monellin: Insights from circular permutated mutants.
Journal, issue, pagesInt. J. Biol. Macromol., Vol. 308, Page 142239-142239, Year 2025
Publish dateNov 26, 2024 (structure data deposition date)
AuthorsLucignano, R. / Bologna, A. / Gramazio, S. / Wang, P.H. / Taxis, C. / Essen, L.O. / Picone, D. / Spadaccini, R.
External linksInt. J. Biol. Macromol. / PubMed:40118405
MethodsX-ray diffraction
Resolution1.15 - 1.6 Å
Structure data

PDB-9hij:
X-ray structure of Perm1, a circularly permuted mutant of the sweet protein MNEI
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-9hik:
X-ray structure of Perm3, a circularly permuted mutant of the sweet protein MNEI
Method: X-RAY DIFFRACTION / Resolution: 1.15 Å

PDB-9hkg:
X-ray structure of Perm2, a circularly permuted mutant of the sweet protein MNEI
Method: X-RAY DIFFRACTION / Resolution: 1.26 Å

Chemicals

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

ChemComp-ACT:
ACETATE ION

ChemComp-MG:
Unknown entry

ChemComp-P6G:
HEXAETHYLENE GLYCOL / precipitant*YM

ChemComp-HOH:
WATER

ChemComp-ACY:
ACETIC ACID

Source
  • dioscoreophyllum cumminsii (serendipity berry)
KeywordsPLANT PROTEIN / sweet protein

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