1tuk: Difference between revisions

[[Image:1tuk.gif|left|200px]]<br /><applet load="1tuk" size="350" color="white" frame="true" align="right" spinBox="true"  

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.

1TUK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum] with <scene name='pdbligand=IOD:'>IOD</scene> and <scene name='pdbligand=PGM:'>PGM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TUK OCA].  

[[Category: Gautier, M F.]]

[[Category: Lamotte, F De.]]

[[Category: Pons, J L.]]

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