2r74

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(New page: 200px<br /><applet load="2r74" size="350" color="white" frame="true" align="right" spinBox="true" caption="2r74, resolution 1.900&Aring;" /> '''Crystal Structure o...)
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==Overview==
==Overview==
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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 crystallized 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 (1 A=0.1 nm) 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 previously. 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 crystallization medium. Trichosurin was also, co-crystallized 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.
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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 crystallized 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 (1 A=0.1 nm) 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 previously. 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 crystallization medium. Trichosurin was also co-crystallized 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.
==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Trichosurus vulpecula]]
[[Category: Trichosurus vulpecula]]
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[[Category: Watson, R.P.]]
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[[Category: Watson, R P.]]
[[Category: CL]]
[[Category: CL]]
[[Category: IPA]]
[[Category: IPA]]
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[[Category: transport protein]]
[[Category: transport protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:10:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:45:12 2008''

Revision as of 16:45, 21 February 2008

Image:2r74.jpg

2r74, resolution 1.900Å

Drag the structure with the mouse to rotate

Crystal Structure of the Possum Milk Whey Lipocalin Trichosurin at pH 4.6

Overview

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 crystallized 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 (1 A=0.1 nm) 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 previously. 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 crystallization medium. Trichosurin was also co-crystallized 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.

About this Structure

2R74 is a Single protein structure of sequence from Trichosurus vulpecula with , and as ligands. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure and ligand binding properties of trichosurin, a metatherian lipocalin from the milk whey of the common brushtail possum Trichosurus vulpecula., Watson RP, Demmer J, Baker EN, Arcus VL, Biochem J. 2007 Nov 15;408(1):29-38. PMID:17685895

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