2r74
From Proteopedia
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|PDB= 2r74 |SIZE=350|CAPTION= <scene name='initialview01'>2r74</scene>, resolution 1.900Å | |PDB= 2r74 |SIZE=350|CAPTION= <scene name='initialview01'>2r74</scene>, resolution 1.900Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2r73|2R73]], [[2ra6|2RA6]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2r74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r74 OCA], [http://www.ebi.ac.uk/pdbsum/2r74 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2r74 RCSB]</span> | ||
}} | }} | ||
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[[Category: Trichosurus vulpecula]] | [[Category: Trichosurus vulpecula]] | ||
[[Category: Watson, R P.]] | [[Category: Watson, R P.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: IPA]] | ||
| - | [[Category: ZN]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
[[Category: dimer]] | [[Category: dimer]] | ||
| Line 36: | Line 36: | ||
[[Category: transport protein]] | [[Category: transport protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:57:15 2008'' |
Revision as of 01:57, 31 March 2008
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| , resolution 1.900Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 2R73, 2RA6
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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