4jru

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

spinqualitylabelsall models 4jru, resolution 1.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4jru is a 1 chain structure with sequence from Vitis vinifera. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.2Å Ligands: GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function F6HUG9_VITVI Publication Abstract from PubMed 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 degrees 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. Structure of Haze Forming Proteins in White Wines: Vitis vinifera Thaumatin-Like Proteins.,Marangon M, Van Sluyter SC, Waters EJ, Menz RI PLoS One. 2014 Dec 2;9(12):e113757. doi: 10.1371/journal.pone.0113757., eCollection 2014. PMID:25463627 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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