1tuk

Crystal stucture of liganted type 2 non specific lipid transfer protein from wheat

spinqualitylabelsall models 1tuk, resolution 1.12Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1tuk is a 1 chain structure with sequence from Triticum aestivum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: IOD, PGM Related: 1n89 Resources: FirstGlance, OCA, RCSB, PDBsum Function [NLT2G_WHEAT] Transfer lipids across membranes. May play a role in plant defense or in the biosynthesis of cuticle layers. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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