2BV7

Crystal structure of GLTP with bound GM3

Summary for 2BV7

• Entry DOI: 10.2210/pdb2bv7/pdb
• Related: 1TFJ 1WBE
• Descriptor: GLYCOLIPID TRANSFER PROTEIN, SULFATE ION, N-{1-[(HEXOPYRANOSYLOXY)METHYL]-2-HYDROXYNONADECYL}TETRACOSANAMIDE, ... (4 entities in total)
• Functional Keywords: glycolipid, ligand binding, acetylation, lipid transport, transport, glycolipid transfer protein
• Biological source: BOS TAURUS (BOVINE)
• Cellular location: Cytoplasm (By similarity): P68265
• Total number of polymer chains: 1
• Total formula weight: 24854.11

Authors

Kidron, H.,Airenne, T.T.,Nymalm, Y.,Nylund, M.,West, G.,Mattjus, P.,Salminen, T.A. (deposition date: 2005-06-23, release date: 2005-12-14, Last modification date: 2023-12-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.79 Å)