1tuk: Difference between revisions
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New page: left|200px<br /><applet load="1tuk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tuk, resolution 1.12Å" /> '''Crystal stucture of ... |
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== | ==Crystal structure of liganded type 2 non specific lipid transfer protein from wheat== | ||
In plants, a family of ubiquitous proteins named non-specific | <StructureSection load='1tuk' size='340' side='right'caption='[[1tuk]], [[Resolution|resolution]] 1.12Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1tuk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TUK 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]] 1.12Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=PGM:1-MYRISTOYL-2-HYDROXY-SN-GLYCERO-3-[PHOSPHO-RAC-(1-GLYCEROL)]'>PGM</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=1tuk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tuk OCA], [https://pdbe.org/1tuk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tuk RCSB], [https://www.ebi.ac.uk/pdbsum/1tuk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tuk ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/NLT2G_WHEAT NLT2G_WHEAT] Transfer lipids across membranes. May play a role in plant defense or in the biosynthesis of cuticle layers.<ref>PMID:11231292</ref> | |||
== 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/tu/1tuk_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=1tuk ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In plants, a family of ubiquitous proteins named non-specific lipid-transfer proteins (ns-LTPs) facilitates the transfer of fatty acids, phospholipids and steroids between membranes. Recent data suggest that these secreted proteins play a key role in the formation of cuticular wax layers and in defence mechanisms against pathogens. In this study, X-ray crystallography has been used to examine the structural details of the interaction between a wheat type 2 ns-LTP and a lipid, L-alpha-palmitoyl-phosphatidyl glycerol. This crystal structure was solved ab initio at 1.12 A resolution by direct methods. The typical alpha-helical bundle fold of this protein is maintained by four disulfide bridges and delineates two hydrophobic cavities. The inner surface of the main cavity is lined by non-polar residues that provide a hydrophobic environment for the palmitoyl moiety of the lipid. The head-group region of this lipid protrudes from the surface and makes several polar interactions with a conserved patch of basic residues at the entrance of the pocket. The alkyl chain of a second lipid is bound within an adjacent smaller cavity. The structure shows that binding of the lipid tails to the protein involves extensive hydrophobic interactions. | |||
Structure of a liganded type 2 non-specific lipid-transfer protein from wheat and the molecular basis of lipid binding.,Hoh F, Pons JL, Gautier MF, de Lamotte F, Dumas C Acta Crystallogr D Biol Crystallogr. 2005 Apr;61(Pt 4):397-406. Epub 2005, Mar 24. PMID:15805594<ref>PMID:15805594</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 1tuk" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Triticum aestivum]] | [[Category: Triticum aestivum]] | ||
[[Category: | [[Category: De Lamotte F]] | ||
[[Category: | [[Category: Dumas C]] | ||
[[Category: | [[Category: Gautier MF]] | ||
[[Category: | [[Category: Hoh F]] | ||
[[Category: Pons | [[Category: Pons JL]] | ||
Latest revision as of 07:29, 30 October 2024
Crystal structure of liganded type 2 non specific lipid transfer protein from wheat
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