5TVI

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

5TVI の概要

• エントリーDOI: 10.2210/pdb5tvi/pdb
• 分子名称: non specific lipid transfer protein, GLYCEROL, MYRISTIC ACID, ... (5 entities in total)
• 機能のキーワード: solanum melongena, non-specific lipid transfer protein, plant protein
• 由来する生物種: Solanum melongena (eggplant)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19540.46

構造登録者

Jain, A.,Salunke, D.M. (登録日: 2016-11-09, 公開日: 2017-07-05, 最終更新日: 2024-10-16)

主引用文献

Jain, A.,Salunke, D.M.
Crystal structure of nonspecific lipid transfer protein from Solanum melongena
Proteins, 85:1820-1830, 2017

PubMed Abstract: 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 Å resolution. Overall, the tertiary structure is a cluster of α-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.

PubMed: 28612368
DOI: 10.1002/prot.25335

実験手法

X-RAY DIFFRACTION (1.87 Å)