5tvi | pdb_00005tvi

Crystal structure of non-specific lipid transfer protein reveals non-canonical lipid binding: possible relevance in modulating allergenicity

spinqualitylabelsall models 5tvi, resolution 1.87Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5tvi is a 2 chain structure with sequence from Solanum virginianum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.87Å Ligands: GOL, MYR, O8N Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A247D6Y2_SOLME Publication Abstract from PubMed Lipids are considered to protect protein allergens from proteolysis and are generally seen to exist in a bound form. One of the well-known plant protein families with bound lipids is non-specific lipid transfer proteins (nsLTPs). Structure-function relationships in the case of the members of non-specific lipid transfer protein family are not clearly understood. As part of exploring the seed proteome, we have analyzed the proteome of a member of Solanaceae family, Solanum melongena (eggplant) and a non-specific lipid transfer protein from S. melongena, SM80.2 was purified, crystallized and the structure was determined at 1.87 A resolution. Overall, the tertiary structure is a cluster of alpha-helices forming an internal hydrophobic cavity. Absence of conserved Tyr79, known to govern the plasticity of hydrophobic cavity, and formation of hydrogen bond between Asn79 and Asn36 further reduced the pocket size. Structural analysis of SM80.2 thus gives insight about a new hydrogen bond mediated mechanism followed in closure of the binding pocket. Extra electron densities observed at two different places on the protein surface and not in the cavity could provide interesting physiological relevance. In light of allergenic properties, probably overlapping of epitopic region and ligand binding on surface could be a main reason. This work shows first crystal structure of A-like nsLTP with a close binding pocket and extra density on the surface suggesting a plausible intermediate state during transfer. Crystal structure of nonspecific lipid transfer protein from Solanum melongena.,Jain A, Salunke DM Proteins. 2017 Oct;85(10):1820-1830. doi: 10.1002/prot.25335. Epub 2017 Jun 27. PMID:28612368 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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