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1N89

Solution structure of a liganded type 2 wheat non-specific Lipid Transfer Protein

1N89 の概要
エントリーDOI10.2210/pdb1n89/pdb
NMR情報BMRB: 4977
分子名称lipid transfer protein, 1-MYRISTOYL-2-HYDROXY-SN-GLYCERO-3-[PHOSPHO-RAC-(1-GLYCEROL)] (2 entities in total)
機能のキーワードlipid transfer protein, lipid transport
由来する生物種Triticum turgidum subsp. durum (durum wheat)
タンパク質・核酸の鎖数1
化学式量合計7469.50
構造登録者
Pons, J.L.,de Lamotte, F.,Gautier, M.F.,Delsuc, M.A. (登録日: 2002-11-20, 公開日: 2003-03-18, 最終更新日: 2023-06-14)
主引用文献Pons, J.L.,de Lamotte, F.,Gautier, M.F.,Delsuc, M.A.
Refined solution structure of a liganded type 2 wheat nonspecific lipid transfer protein.
J.Biol.Chem., 278:14249-14256, 2003
Cited by
PubMed Abstract: The refined structure of a wheat type 2 nonspecific lipid transfer protein (ns-LTP2) liganded with l-alpha-palmitoylphosphatidylglycerol has been determined by NMR. The (15)N-labeled protein was produced in Pichia pastoris. Physicochemical conditions and ligandation were intensively screened to obtain the best NMR spectra quality. This ns-LTP2 is a 67-residue globular protein with a diameter of about 30 A. The structure is composed of five helices forming a right superhelix. The protein presents an inner cavity, which has been measured at 341 A(3). All of the helices display hydrophobic side chains oriented toward the cavity. The phospholipid is found in this cavity. Its fatty acid chain is completely inserted in the protein, the l-alpha-palmitoylphosphatidylglycerol glycerol moiety being located on a positively charged pocket on the surface of the protein. The superhelix structure of the protein is coiled around the fatty acid chain. The overall structure shows similarities with ns-LTP1. Nevertheless, large three-dimensional structural discrepancies are observed for the H3 and H4 alpha-helices, the C-terminal region, and the last turn of the H2 helix. The lipid is orthogonal to the orientation observed in ns-LTP1. The volume of the hydrophobic cavity appears to be in the same range as the one of ns-LTP1, despite the fact that ns-LTP2 is shorter by 24 residues.
PubMed: 12525478
DOI: 10.1074/jbc.M211683200
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 1n89
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-13に公開中

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