1gh1
From Proteopedia
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NMR STRUCTURES OF WHEAT NONSPECIFIC LIPID TRANSFER PROTEIN
Overview
Two-dimensional and three-dimensional 1H-NMR experimental data [Simorre, J. P., Caille, A., Marion, D., Marion, D. & Ptak, M. (1991) Biochemistry, 30, 11600-11608] were used to build models of the three-dimensional, structure of a non-specific wheat lipid-transfer protein (LTP) by using, distance geometry, simulated annealing, energy minimization and molecular, dynamics techniques. A first set of 881 distance constraints derived from, NOE cross-peak intensities was used to generate 74 initial structures. One, family of topological mirror images of the protein structure was, eliminated by considering helical secondary-structure organization and, steric requirements. Back calculations of NOE intensities led us to, introduce 535 additional distance constraints. Finally, 21 structures were, selected as representative of the structure of the protein. The, polypeptide backbone folds into a simple and original right-handed, winding. It is composed of a bundle of four helices linked by flexible, loops, which is packed against a C-terminal fragment forming a, non-standard saxophone-like shape. The folded protein is stabilized by, hydrophobic interactions and the four disulfide bridges combined by pairs, on each side of the protein. An hydrophobic cleft, formed by residues, located in the second half of the protein could be a potential site for, the binding of lipids.
About this Structure
1GH1 is a Single protein structure of sequence from Triticum aestivum. This structure superseeds the now removed PDB entry 1LPT. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure in solution of a wheat lipid-transfer protein from multidimensional 1H-NMR data. A new folding for lipid carriers., Gincel E, Simorre JP, Caille A, Marion D, Ptak M, Vovelle F, Eur J Biochem. 1994 Dec 1;226(2):413-22. PMID:8001559
Page seeded by OCA on Tue Nov 20 16:03:07 2007
