4L5H

Structure of haze forming proteins in white wines: Vitis vinifera thaumatin-like proteins

Replaces:  4H8T

Summary for 4L5H

• Entry DOI: 10.2210/pdb4l5h/pdb
• Related: 4JRU
• Descriptor: VVTL1, GLYCEROL (3 entities in total)
• Functional Keywords: antifungal protein, plant protein
• Biological source: Vitis vinifera (Grape)
• Total number of polymer chains: 2
• Total formula weight: 42695.31

Authors

Marangon, M.,Menz, R.I.,Waters, E.J.,Van Sluyter, S.C. (deposition date: 2013-06-11, release date: 2013-07-03, Last modification date: 2023-09-20)

Primary citation

Marangon, M.,Van Sluyter, S.C.,Waters, E.J.,Menz, R.I.
Structure of Haze Forming Proteins in White Wines: Vitis vinifera Thaumatin-Like Proteins.
Plos One, 9:e113757-e113757, 2014

PubMed Abstract: Grape thaumatin-like proteins (TLPs) play roles in plant-pathogen interactions and can cause protein haze in white wine unless removed prior to bottling. Different isoforms of TLPs have different hazing potential and aggregation behavior. Here we present the elucidation of the molecular structures of three grape TLPs that display different hazing potential. The three TLPs have very similar structures despite belonging to two different classes (F2/4JRU is a thaumatin-like protein while I/4L5H and H2/4MBT are VVTL1), and having different unfolding temperatures (56 vs. 62°C), with protein F2/4JRU being heat unstable and forming haze, while I/4L5H does not. These differences in properties are attributable to the conformation of a single loop and the amino acid composition of its flanking regions.

PubMed: 25463627
DOI: 10.1371/journal.pone.0113757

Experimental method

X-RAY DIFFRACTION (1.8 Å)