Thu, 21 Aug 2008 06:23:59 BST CiteULike: 著者: Arcus http://www.citeulike.org/author/Arcus CiteULike.org en-gb Copyright © 2004-2008 citeulike.org http://www.citeulike.org/user/neils/article/2643444 <i>Proteins: Structure, Function, and Bioinformatics, Vol. 9999, No. 9999. (2008), NA.</i><br /><br />No abstract. Crystal structure of PAE0151 from <I>Pyrobaculum aerophilum</I>, a PIN-domain (VapC) protein from a toxin-antitoxin operon Richard Bunker Joanna Mckenzie Edward Baker Vickery Arcus doi:10.1002/prot.22048 Proteins: Structure, Function, and Bioinformatics, Vol. 9999, No. 9999. (2008), NA. 2008-04-09T03:12:58-00:00 2008 Proteins: Structure, Function, and Bioinformatics 9999 9999 NA antitoxin archaea crystallography protein pyrobaculum structure toxin http://www.citeulike.org/user/dimka/article/1753808 <i>Biochem J (8 August 2007)</i><br /><br />Lipocalins are extracellular proteins (17-25 kDa) that bind and transport small lipophilic molecules. The three dimensional structure of the first lipocalin from a metatherian has been determined at different values of pH both with and without bound ligands. Trichosurin, a protein from the milk whey of the common brushtail possum, Trichosurus vulpecula, has been recombinantly expressed in Escherichia coli, refolded from inclusion bodies, purified and crystallised at two different pH values. The three-dimensional structure of trichosurin was solved by X-ray crystallography in two different crystal forms to 1.9 A and 2.6 A resolution, from crystals grown at low and high pH values, respectively. Trichosurin has the typical lipocalin fold - an eight stranded, anti parallel, beta-barrel but dimerizes in an orientation that has not been seen before. The putative binding pocket in the centre of the beta-barrel is well defined in both high and low pH structures and is occupied by water molecules along with isopropanol molecules from the crystallisation media. Trichosurin was also co-crystallised with a number of small molecule ligands and structures were determined with 2-naphthol and 4-ethylphenol bound in the centre of the beta-barrel. The binding of phenolic compounds by trichosurin provides clues to the function of this important marsupial-milk protein, which is highly conserved across metatherians. Three-dimensional structure and ligand binding properties of Trichosurin, a metatherian lipocalin from the milk whey of the common brushtail possum, Trichosurus vulpecula. Randall Watson Jerome Demmer Edward Baker Vickery Arcus doi:10.1042/BJ20070567 Biochem J (8 August 2007) 2007-10-11T05:42:12-00:00 2007 Biochem J 1470-8728 mmult-ref