2mal

Publication Abstract from PubMed

Lipid transfer protein, designated as Lc-LTP2, was isolated from seeds of the lentil Lens culinaris. The protein has molecular mass 9282.7Da, consists of 93 amino acid residues including 8 cysteines forming 4 disulfide bonds. Lc-LTP2 and its stable isotope labeled analogues were overexpressed in Escherichia coli and purified. Antimicrobial activity of the recombinant protein was examined, and its spatial structure was studied by NMR spectroscopy. The polypeptide chain of Lc-LTP2 forms four alpha-helices (Cys4-Leu18, Pro26-Ala37, Thr42-Ala56, Thr64-Lys73) and a long C-terminal tail without regular secondary structure. Side chains of the hydrophobic residues form a relatively large internal tunnel-like lipid-binding cavity (van der Waals volume comes up to approximately 600A3). The side-chains of Arg45, Pro79, and Tyr80 are located near an assumed mouth of the cavity. Titration with dimyristoyl phosphatidylglycerol (DMPG) revealed formation of the Lc-LTP2/lipid non-covalent complex accompanied by rearrangements in the protein spatial structure and expansion of the internal cavity. The resultant Lc-LTP2/DMPG complex demonstrates limited lifetime and dissociates within tens of hours.

Recombinant production and solution structure of lipid transfer protein from lentil Lens culinaris.,Gizatullina AK, Finkina EI, Mineev KS, Melnikova DN, Bogdanov IV, Telezhinskaya IN, Balandin SV, Shenkarev ZO, Arseniev AS, Ovchinnikova TV Biochem Biophys Res Commun. 2013 Aug 31. pii: S0006-291X(13)01425-3. doi:, 10.1016/j.bbrc.2013.08.078. PMID:23998937^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.