1WBE

X-ray structure of bovine GLTP

1WBE の概要

• エントリーDOI: 10.2210/pdb1wbe/pdb
• 関連するPDBエントリー: 1TFJ 2BV7
• 分子名称: GLYCOLIPID TRANSFER PROTEIN, DECANOIC ACID, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: glycolipid transfer protein, glycolipid transfer, acetylation, lipid transport
• 由来する生物種: BOS TAURUS (BOVINE)
• 細胞内の位置: Cytoplasm : P68265
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24215.21

構造登録者

Airenne, T.T.,Kidron, H.,West, G.,Nymalm, Y.,Nylund, M.,Mattjus, P.,Salminen, T.A. (登録日: 2004-11-01, 公開日: 2005-11-30, 最終更新日: 2023-12-13)

主引用文献

Airenne, T.T.,Kidron, H.,Nymalm, Y.,Nylund, M.,West, G.,Mattjus, P.,Salminen, T.A.
Structural Evidence for Adaptive Ligand Binding of Glycolipid Transfer Protein.
J.Mol.Biol., 355:224-, 2006

PubMed Abstract: Glycolipids participate in many important cellular processes and they are bound and transferred with high specificity by glycolipid transfer protein (GLTP). We have solved three different X-ray structures of bovine GLTP at 1.4 angstroms, 1.6 angstroms and 1.8 angstroms resolution, all with a bound fatty acid or glycolipid. The 1.4 angstroms structure resembles the recently characterized apo-form of the human GLTP but the other two structures represent an intermediate conformation of the apo-GLTPs and the human lactosylceramide-bound GLTP structure. These novel structures give insight into the mechanism of lipid binding and how GLTP may conformationally adapt to different lipids. Furthermore, based on the structural comparison of the GLTP structures and the three-dimensional models of the related Podospora anserina HET-C2 and Arabidopsis thaliana accelerated cell death protein, ACD11, we give structural explanations for their specific lipid binding properties.

PubMed: 16309699
DOI: 10.1016/J.JMB.2005.10.031

実験手法

X-RAY DIFFRACTION (1.36 Å)