1UVC

Lipid Binding in Rice Nonspecific Lipid Transfer Protein-1 Complexes from Oryza sativa

1UVC の概要

• エントリーDOI: 10.2210/pdb1uvc/pdb
• 関連するPDBエントリー: 1BV2 1MZM 1RZL 1UVA 1UVB
• 分子名称: NONSPECIFIC LIPID TRANSFER PROTEIN, STEARIC ACID (3 entities in total)
• 機能のキーワード: lipid transport, ltp 1, pap 1, rice, fatty acid binding
• 由来する生物種: ORYZA SATIVA (RICE)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18407.33

構造登録者

Cheng, H.-C.,Cheng, P.-T.,Peng, P.,Lyu, P.-C.,Sun, Y.-J. (登録日: 2004-01-19, 公開日: 2004-10-19, 最終更新日: 2024-11-06)

主引用文献

Cheng, H.-C.,Cheng, P.-T.,Peng, P.,Lyu, P.-C.,Sun, Y.-J.
Lipid Binding in Rice Nonspecific Lipid Transfer Protein-1 Complexes from Oryza Sativa
Protein Sci., 13:2304-, 2004

PubMed Abstract: Nonspecific lipid transfer proteins (nsLTPs) facilitate the transfer of phospholipids, glycolipids, fatty acids and steroids between membranes, with wide-ranging binding affinities. Three crystal structures of rice nsLTP1 from Oryza sativa, complexed with myristic (MYR), palmitic (PAL) or stearic acid (STE) were determined. The overall structures of the rice nsLTP1 complexes belong to the four-helix bundle folding with a long C-terminal loop. The nsLTP1-MYR and the nsLTP1-STE complexes bind a single fatty acid while the nsLTP1-PAL complex binds two molecules of fatty acids. The C-terminal loop region is elastic in order to accommodate a diverse range of lipid molecules. The lipid molecules interact with the nsLTP1-binding cavity mainly with hydrophobic interactions. Significant conformational changes were observed in the binding cavity and the C-terminal loop of the rice nsLTP1 upon lipid binding.

PubMed: 15295114
DOI: 10.1110/PS.04799704

実験手法

X-RAY DIFFRACTION (2 Å)