1SIY

NMR structure of mung bean non-specific lipid transfer protein 1

1SIY の概要

• エントリーDOI: 10.2210/pdb1siy/pdb
• NMR情報: BMRB: 6089
• 分子名称: Nonspecific lipid-transfer protein 1 (1 entity in total)
• 機能のキーワード: alpha helix, lipid binding protein
• 由来する生物種: Vigna radiata var. radiata (mung bean)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9307.73

構造登録者

Lin, K.F.,Liu, Y.N.,Hsu, S.T.D.,Samuel, D.,Cheng, C.S.,Bonvin, A.M.J.J.,Lyu, P.C. (登録日: 2004-03-02, 公開日: 2005-04-05, 最終更新日: 2024-10-23)

主引用文献

Lin, K.F.,Liu, Y.N.,Hsu, S.T.D.,Samuel, D.,Cheng, C.S.,Bonvin, A.M.J.J.,Lyu, P.C.
Characterization and Structural Analyses of Nonspecific Lipid Transfer Protein 1 from Mung Bean
Biochemistry, 44:5703-5712, 2005

PubMed Abstract: Plant nonspecific lipid transfer proteins (nsLTPs) are thermal stable proteins that are capable of transferring lipid molecules between bilayers in vitro. This family of proteins, abundant in plants, is proposed to be involved in defense, pollination, and germination; the in vivo biological function remains, however, elusive. Here we report the purification and sequencing of an nsLTP1 from mung bean sprouts. We have also determined the solution structure of this nsLTP1, which represents the first 3D structure of the dicotyledonous nsLTP1 family. The global fold of mung bean nsLTP1 is similar to those of the monocotyledonous nsLTP1 structures and consists of four alpha-helices stabilized by four disulfide bonds. There are, however, some notable differences in the C-terminal tails and internal hydrophobic cavities. Circular dichroism and fluorescence spectroscopy were used to compare the thermodynamics and lipid transfer properties of mung bean nsLTP1 with those of rice nsLTP1. Docking of a lipid molecule into the solution structure of mung bean nsLTP1 reveals similar binding cavities and hydrophobic interactions as in rice nsLTP1, consistent with their comparable lipid transfer properties measured experimentally.

PubMed: 15823028
DOI: 10.1021/bi047608v

実験手法

SOLUTION NMR