1rzl

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[[Image:1rzl.jpg|left|200px]]<br /><applet load="1rzl" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1rzl.jpg|left|200px]]
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caption="1rzl, resolution 1.6&Aring;" />
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'''RICE NONSPECIFIC LIPID TRANSFER PROTEIN'''<br />
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{{Structure
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|PDB= 1rzl |SIZE=350|CAPTION= <scene name='initialview01'>1rzl</scene>, resolution 1.6&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=CXS:3-CYCLOHEXYL-1-PROPYLSULFONIC ACID'>CXS</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''RICE NONSPECIFIC LIPID TRANSFER PROTEIN'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1RZL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryza_sativa Oryza sativa] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=CXS:'>CXS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RZL OCA].
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1RZL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryza_sativa Oryza sativa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RZL OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9512714 9512714]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9512714 9512714]
[[Category: Oryza sativa]]
[[Category: Oryza sativa]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: lipid transport]]
[[Category: lipid transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:56:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:58:28 2008''

Revision as of 11:58, 20 March 2008


PDB ID 1rzl

Drag the structure with the mouse to rotate
, resolution 1.6Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



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. 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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