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1tuk
From Proteopedia
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Crystal stucture of liganted type 2 non specific lipid transfer protein from wheat
Overview
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.
About this Structure
1TUK is a Single protein structure of sequence from Triticum aestivum with IOD and PGM as ligands. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Nov 21 03:36:12 2007
