1rzl
From Proteopedia
RICE NONSPECIFIC LIPID TRANSFER PROTEIN
Structural highlights
FunctionNLTP1_ORYSJ Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThis 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
Categories: Large Structures | Oryza sativa | Cha H | Hwang KY | Lee JY | Min KS | Shin DH | Suh SW