1rzl

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spinqualitylabelsall models 1rzl, resolution 1.6Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

RICE NONSPECIFIC LIPID TRANSFER PROTEIN

Overview

This study describes the high-resolution X-ray structure of the, non-specific lipid transfer protein (ns-LTP) from rice seeds in the, unliganded state. The model has been refined to a crystallographic, R-factor of 0.186 for 8.0 to 1.6 A data (with Fo > 2 sigma F). It accounts, for all 91 amino acid residues, 68 water molecules, one sulfate ion, and, two molecules of 3-[cyclohexylamino]-1-propanesulfonic acid. The, root-mean-square deviations from ideal bond lengths and angles are 0.017 A, and 1.76 degrees, respectively. The overall fold of rice ns-LTP is very, similar to that of maize ns-LTP. A superposition of 91 common C alpha, atoms in rice and maize ns-LTPs, both in the unliganded state, gives a, root-mean-square deviation of 1.2 A. Large structural differences from the, crystal structure of maize ns-LTP are observed in two regions: the loop, between two alpha-helices H1 and H2, where one residue deletion (Gln21 of, maize sequence) occurs, and the C-terminal region around Tyr79. The, C-terminal region of rice protein is somewhat collapsed into the, hydrophobic cavity. As a consequence, its hydrophobic cavity is, considerably smaller than that of maize protein (144 A3 versus 408 A3 for, van der Waals cavity volumes), despite a high level of sequence identity, (79%) between them. In the rice ns-LTP structure, the side-chain of Arg44, partially blocks the mouth of the cavity, while the side-chain of Ile81, effectively closes the other end by protruding into the cavity. And the, side-chain of Tyr79 divides the cavity into two parts, with the larger, part being shielded from the solvent. The present study illuminates the, structure-function relationship of rice ns-LTP and allows a detailed, structural comparison with other plant ns-LTPs.

About this Structure

1RZL is a Single protein structure of sequence from Oryza sativa with SO4 and CXS as ligands. Full crystallographic information is available from OCA.

Reference

Rice non-specific lipid transfer protein: the 1.6 A crystal structure in the unliganded state reveals a small hydrophobic cavity., Lee JY, Min K, Cha H, Shin DH, Hwang KY, Suh SW, J Mol Biol. 1998 Feb 20;276(2):437-48. PMID:9512714

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