1l6h
From Proteopedia
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Solution Structure of Plant nsLTP2 purified from Rice (oryza Sativa)
Overview
The three-dimensional structure of rice nonspecific lipid transfer protein, (nsLTP2) has been solved for the first time. The structure of nsLTP2 was, obtained using 813 distance constraints, 30 hydrogen bond constraints, and, 19 dihedral angle constraints. Fifteen of the 50 random simulated, annealing structures satisfied all of the constraints and possessed good, nonbonded contacts. The novel three-dimensional fold of rice nsLTP2, contains a triangular hydrophobic cavity formed by three prominent, helices. The four disulfide bonds required for stabilization of the nsLTP2, structure show a different pattern of cysteine pairing compared with, nsLTP1. The C terminus of the protein is very flexible and forms a cap, over the hydrophobic cavity. Molecular modeling studies suggested that the, hydrophobic cavity could accommodate large molecules with rigid, structures, such as sterols. The positively charged residues on the, molecular surface of nsLTP2 are structurally similar to other plant, defense proteins.
About this Structure
1L6H is a Single protein structure of sequence from Oryza sativa. Full crystallographic information is available from OCA.
Reference
Solution structure of plant nonspecific lipid transfer protein-2 from rice (Oryza sativa)., Samuel D, Liu YJ, Cheng CS, Lyu PC, J Biol Chem. 2002 Sep 20;277(38):35267-73. Epub 2002 May 13. PMID:12011089
Page seeded by OCA on Tue Nov 20 20:19:00 2007
