1rzl
From Proteopedia
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|PDB= 1rzl |SIZE=350|CAPTION= <scene name='initialview01'>1rzl</scene>, resolution 1.6Å | |PDB= 1rzl |SIZE=350|CAPTION= <scene name='initialview01'>1rzl</scene>, resolution 1.6Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CXS:3-CYCLOHEXYL-1-PROPYLSULFONIC+ACID'>CXS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rzl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rzl OCA], [http://www.ebi.ac.uk/pdbsum/1rzl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rzl RCSB]</span> | ||
}} | }} | ||
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[[Category: Shin, D H.]] | [[Category: Shin, D H.]] | ||
[[Category: Suh, S W.]] | [[Category: Suh, S W.]] | ||
| - | [[Category: CXS]] | ||
| - | [[Category: SO4]] | ||
[[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 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:35:15 2008'' |
Revision as of 20:35, 30 March 2008
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| , resolution 1.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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