1tuk

<table><tr><td colspan='2'>[[1tuk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Canadian_hard_winter_wheat Canadian hard winter wheat]. 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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1n89|1n89]]</div></td></tr>

[[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>

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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1tuk" style="background-color:#fffaf0;"></div>

[[Category: Canadian hard winter wheat]]

[[Category: Dumas, C]]

[[Category: Hoh, F]]

[[Category: Lamotte, F De]]

[[Category: Pons, J L]]

[[Category: Lipid transfer protein]]

[[Category: Lipid transport]]

[[Category: Ns-ltp2]]