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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr>

[[https://www.uniprot.org/uniprot/NLTP_MAIZE NLTP_MAIZE]] 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.

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== Publication Abstract from PubMed ==

BACKGROUND: The movement of lipids between membranes is aided by lipid-transfer proteins (LTPs). Some LTPs exhibit broad specificity, transferring many classes of lipids, and are termed non-specific LTPs (ns-LTPs). Despite their apparently similar mode of action, no sequence homology exists between mammalian and plant ns-LTPs and no three-dimensional structure has been reported for any plant ns-LTP. RESULTS: We have determined the crystal structure of ns-LTP from maize seedlings by multiple isomorphous replacement and refined the structure to 1.9 A resolution. The protein comprises a single compact domain with four alpha-helices and a long C-terminal region. The eight conserved cysteines form four disulfide bridges (assigned as Cys4-Cys52, Cys14-Cys29, Cys30-Cys75, and Cys50-Cys89) resolving the ambiguity that remained from the chemical determination of pairings in the homologous protein from castor bean. Two of the bonds, Cys4-Cys52 and Cys50-Cys89, differ from what would have been predicted from sequence alignment with soybean hydrophobic protein. The complex between maize ns-LTP and hexadecanoate (palmitate) has also been crystallized and its structure refined to 1.8 A resolution. CONCLUSIONS: The fold of maize ns-LTP places it in a new category of all-alpha-type structure, first described for soybean hydrophobic protein. In the absence of a bound ligand, the protein has a tunnel-like hydrophobic cavity, which is large enough to accommodate a long fatty acyl chain. In the structure of the complex with palmitate, most of the acyl chain is buried inside this hydrophobic cavity.

High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings.,Shin DH, Lee JY, Hwang KY, Kim KK, Suh SW Structure. 1995 Feb 15;3(2):189-99. PMID:7735835<ref>PMID:7735835</ref>

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

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== References ==

<references/>

[[Category: Lee, J Y]]

[[Category: Shin, D H]]

[[Category: Suh, S W]]

[[Category: Lipid transport]]