1TUK

Crystal structure of liganded type 2 non specific lipid transfer protein from wheat

1TUK の概要

• エントリーDOI: 10.2210/pdb1tuk/pdb
• 関連するPDBエントリー: 1N89
• 分子名称: Nonspecific lipid-transfer protein 2G, IODIDE ION, 1-MYRISTOYL-2-HYDROXY-SN-GLYCERO-3-[PHOSPHO-RAC-(1-GLYCEROL)], ... (4 entities in total)
• 機能のキーワード: ns-ltp2, lipid transfer protein, lipid transport
• 由来する生物種: Triticum aestivum (bread wheat)
• 細胞内の位置: Secreted, cell wall : P82900
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8206.86

構造登録者

Hoh, F.,Pons, J.L.,Gautier, M.F.,De Lamotte, F.,Dumas, C. (登録日: 2004-06-25, 公開日: 2005-04-05, 最終更新日: 2024-10-30)

主引用文献

Hoh, F.,Pons, J.L.,Gautier, M.F.,de Lamotte, F.,Dumas, C.
Structure of a liganded type 2 non-specific lipid-transfer protein from wheat and the molecular basis of lipid binding.
Acta Crystallogr.,Sect.D, 61:397-406, 2005

PubMed Abstract: In plants, a family of ubiquitous proteins named non-specific lipid-transfer proteins (ns-LTPs) facilitates the transfer of fatty acids, phospholipids and steroids between membranes. Recent data suggest that these secreted proteins play a key role in the formation of cuticular wax layers and in defence mechanisms against pathogens. In this study, X-ray crystallography has been used to examine the structural details of the interaction between a wheat type 2 ns-LTP and a lipid, L-alpha-palmitoyl-phosphatidyl glycerol. This crystal structure was solved ab initio at 1.12 A resolution by direct methods. The typical alpha-helical bundle fold of this protein is maintained by four disulfide bridges and delineates two hydrophobic cavities. The inner surface of the main cavity is lined by non-polar residues that provide a hydrophobic environment for the palmitoyl moiety of the lipid. The head-group region of this lipid protrudes from the surface and makes several polar interactions with a conserved patch of basic residues at the entrance of the pocket. The alkyl chain of a second lipid is bound within an adjacent smaller cavity. The structure shows that binding of the lipid tails to the protein involves extensive hydrophobic interactions.

PubMed: 15805594
DOI: 10.1107/S0907444905000417

実験手法

X-RAY DIFFRACTION (1.12 Å)