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| - | [[Image:1rzl.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1rzl.png|left|200px]] |
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| | {{STRUCTURE_1rzl| PDB=1rzl | SCENE= }} | | {{STRUCTURE_1rzl| PDB=1rzl | SCENE= }} |
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| - | '''RICE NONSPECIFIC LIPID TRANSFER PROTEIN'''
| + | ===RICE NONSPECIFIC LIPID TRANSFER PROTEIN=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9512714}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9512714 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9512714}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Alpha-helical structure]] | | [[Category: Alpha-helical structure]] |
| | [[Category: Lipid transport]] | | [[Category: Lipid transport]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:06:31 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:44:31 2008'' |
Revision as of 20:44, 28 July 2008
Template:STRUCTURE 1rzl
RICE NONSPECIFIC LIPID TRANSFER PROTEIN
Template:ABSTRACT PUBMED 9512714
About this Structure
1RZL is a Single protein structure of sequence from Oryza sativa. 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
Page seeded by OCA on Mon Jul 28 23:44:31 2008
