1rzl
From Proteopedia
(New page: 200px<br /><applet load="1rzl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rzl, resolution 1.6Å" /> '''RICE NONSPECIFIC LIPI...) |
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| - | [[Image:1rzl.jpg|left|200px]]<br /><applet load="1rzl" size=" | + | [[Image:1rzl.jpg|left|200px]]<br /><applet load="1rzl" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rzl, resolution 1.6Å" /> | caption="1rzl, resolution 1.6Å" /> | ||
'''RICE NONSPECIFIC LIPID TRANSFER PROTEIN'''<br /> | '''RICE NONSPECIFIC LIPID TRANSFER PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | This study describes the high-resolution X-ray structure of the | + | 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== | ==About this Structure== | ||
| - | 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 SO4 and CXS as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cha, H.]] | [[Category: Cha, H.]] | ||
| - | [[Category: Hwang, K | + | [[Category: Hwang, K Y.]] |
| - | [[Category: Lee, J | + | [[Category: Lee, J Y.]] |
| - | [[Category: Min, K | + | [[Category: Min, K S.]] |
| - | [[Category: Shin, D | + | [[Category: Shin, D H.]] |
| - | [[Category: Suh, S | + | [[Category: Suh, S W.]] |
[[Category: CXS]] | [[Category: CXS]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: lipid transport]] | [[Category: lipid transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:56:16 2008'' |
Revision as of 12:56, 21 February 2008
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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 and 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
Page seeded by OCA on Thu Feb 21 14:56:16 2008
Categories: Oryza sativa | Single protein | Cha, H. | Hwang, K Y. | Lee, J Y. | Min, K S. | Shin, D H. | Suh, S W. | CXS | SO4 | Alpha-helical structure | Lipid transport
