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

Summary for 3PXM

DescriptorMonellin chain B/Monellin chain A chimeric protein (2 entities in total)
Functional Keywordsa poly-(l-proline) ii (ppii) helix, sweet protein, plant protein
Biological sourceDioscoreophyllum cumminsii (Serendipity berry)
Total number of polymer chains2
Total molecular weight22781.99
Hobbs, J.R.,Templeton, C.M.,Pour, S.O.,Blanch, E.W.,Munger, S.M.,Conn, G.L. (deposition date: 2010-12-10, release date: 2011-04-06, Last modification date: 2017-08-02)
Primary citation
Templeton, C.M.,Ostovar Pour, S.,Hobbs, J.R.,Blanch, E.W.,Munger, S.D.,Conn, G.L.
Reduced Sweetness of a Monellin (MNEI) Mutant Results from Increased Protein Flexibility and Disruption of a Distant Poly-(L-Proline) II Helix.
Chem Senses, 36:425-434, 2011
PubMed: 21343241 (PDB entries with the same primary citation)
DOI: 10.1093/chemse/bjr007
MImport into Mendeley
Experimental method
NMR Information

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.227604.9%3.6%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution