1rzl
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:1rzl.png|left|200px]] | ||
| - | < | + | ==RICE NONSPECIFIC LIPID TRANSFER PROTEIN== |
| - | + | <StructureSection load='1rzl' size='340' side='right'caption='[[1rzl]], [[Resolution|resolution]] 1.60Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[1rzl]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RZL FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | |
| - | -- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CXS:3-CYCLOHEXYL-1-PROPYLSULFONIC+ACID'>CXS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rzl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rzl OCA], [https://pdbe.org/1rzl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rzl RCSB], [https://www.ebi.ac.uk/pdbsum/1rzl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rzl ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/NLTP1_ORYSJ NLTP1_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 Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rz/1rzl_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rzl ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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<ref>PMID:9512714</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1rzl" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | --> | + | <references/> |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: Large Structures]] |
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[[Category: Oryza sativa]] | [[Category: Oryza sativa]] | ||
| - | + | [[Category: Cha H]] | |
| - | [[Category: Cha | + | [[Category: Hwang KY]] |
| - | [[Category: Hwang | + | [[Category: Lee JY]] |
| - | [[Category: Lee | + | [[Category: Min KS]] |
| - | [[Category: Min | + | [[Category: Shin DH]] |
| - | [[Category: Shin | + | [[Category: Suh SW]] |
| - | [[Category: Suh | + | |
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Current revision
RICE NONSPECIFIC LIPID TRANSFER PROTEIN
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Categories: Large Structures | Oryza sativa | Cha H | Hwang KY | Lee JY | Min KS | Shin DH | Suh SW

