1siy

<StructureSection load='1siy' size='340' side='right'caption='[[1siy]], [[NMR_Ensembles_of_Models | 15 NMR models]]' 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=1siy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1siy OCA], [https://pdbe.org/1siy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1siy RCSB], [https://www.ebi.ac.uk/pdbsum/1siy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1siy ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/NLTP1_VIGRR NLTP1_VIGRR]] 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. Has antifungal activity against F.solani, F.oxysporum, P.aphanidermatum and S.rolfsii. Has antibacterial activity against the Gram-positive bacterium S.aureus but not against the Gram-negative bacterium S.typhimurium.<ref>PMID:15350690</ref> <ref>PMID:15823028</ref>

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== Publication Abstract from PubMed ==

Plant nonspecific lipid transfer proteins (nsLTPs) are thermal stable proteins that are capable of transferring lipid molecules between bilayers in vitro. This family of proteins, abundant in plants, is proposed to be involved in defense, pollination, and germination; the in vivo biological function remains, however, elusive. Here we report the purification and sequencing of an nsLTP1 from mung bean sprouts. We have also determined the solution structure of this nsLTP1, which represents the first 3D structure of the dicotyledonous nsLTP1 family. The global fold of mung bean nsLTP1 is similar to those of the monocotyledonous nsLTP1 structures and consists of four alpha-helices stabilized by four disulfide bonds. There are, however, some notable differences in the C-terminal tails and internal hydrophobic cavities. Circular dichroism and fluorescence spectroscopy were used to compare the thermodynamics and lipid transfer properties of mung bean nsLTP1 with those of rice nsLTP1. Docking of a lipid molecule into the solution structure of mung bean nsLTP1 reveals similar binding cavities and hydrophobic interactions as in rice nsLTP1, consistent with their comparable lipid transfer properties measured experimentally.

Characterization and structural analyses of nonspecific lipid transfer protein 1 from mung bean.,Lin KF, Liu YN, Hsu ST, Samuel D, Cheng CS, Bonvin AM, Lyu PC Biochemistry. 2005 Apr 19;44(15):5703-12. PMID:15823028<ref>PMID:15823028</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 1siy" style="background-color:#fffaf0;"></div>

[[Category: Bonvin, A M.J J]]

[[Category: Cheng, C S]]

[[Category: Hsu, S T.D]]

[[Category: Lin, K F]]

[[Category: Liu, Y N]]

[[Category: Lyu, P C]]

[[Category: Samuel, D]]

[[Category: Lipid binding protein]]