1thw
From Proteopedia
(New page: 200px<br /><applet load="1thw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1thw, resolution 1.75Å" /> '''THE STRUCTURES OF TH...) |
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| - | [[Image:1thw.gif|left|200px]]<br /><applet load="1thw" size=" | + | [[Image:1thw.gif|left|200px]]<br /><applet load="1thw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1thw, resolution 1.75Å" /> | caption="1thw, resolution 1.75Å" /> | ||
'''THE STRUCTURES OF THREE CRYSTAL FORMS OF THE SWEET PROTEIN THAUMATIN'''<br /> | '''THE STRUCTURES OF THREE CRYSTAL FORMS OF THE SWEET PROTEIN THAUMATIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Three crystal forms of the sweet-tasting protein thaumatin from the | + | Three crystal forms of the sweet-tasting protein thaumatin from the African berry Thaumatococcus daniellii have been grown. These include two naturally occurring isoforms, A and B, that differ by a single amino acid, and a recombinant form of isoform B expressed in yeast. The crystals are of space groups C2 with a = 117.7, b = 44.9, c = 38.0 A, and beta = 94.0 degrees, P2(1)2(1)2(1) with a = 44.3, b = 63.7 and c = 72.7 A, and a tetragonal form P4(1)2(1)2 with a = b = 58.6 and c = 151.8 A. The structures of all three crystals have been solved by molecular replacement and subsequently refined to R factors of 0.184 for the monoclinic at 2.6 A, 0.165 for the orthorhombic at 1.75 A, and 0.181 for the tetragonal, also at 1.75 A resolution. No solvent was included in the monoclinic crystal while 123 and 105 water molecules were included in the higher resolution orthorhombic and tetragonal structures, respectively. A bound tartrate molecule was also clearly visible in the tetragonal structure. The r.m.s. deviations between molecular structures in the three crystals range from 0.6 to 0.7 A for Calpha atoms, and 1.1 to 1.3 A for all atoms. This is comparable to the r.m.s. deviation between the three structures and the starting model. Nevertheless, several peptide loops show particularly large variations from the initial model. |
==About this Structure== | ==About this Structure== | ||
| - | 1THW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii] with TLA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1THW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii] with <scene name='pdbligand=TLA:'>TLA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1THW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Day, J.]] | [[Category: Day, J.]] | ||
[[Category: Greenwood, A.]] | [[Category: Greenwood, A.]] | ||
| - | [[Category: Ko, T | + | [[Category: Ko, T P.]] |
[[Category: McPherson, A.]] | [[Category: McPherson, A.]] | ||
[[Category: TLA]] | [[Category: TLA]] | ||
[[Category: sweet tasting protein]] | [[Category: sweet tasting protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:13:38 2008'' |
Revision as of 13:13, 21 February 2008
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THE STRUCTURES OF THREE CRYSTAL FORMS OF THE SWEET PROTEIN THAUMATIN
Overview
Three crystal forms of the sweet-tasting protein thaumatin from the African berry Thaumatococcus daniellii have been grown. These include two naturally occurring isoforms, A and B, that differ by a single amino acid, and a recombinant form of isoform B expressed in yeast. The crystals are of space groups C2 with a = 117.7, b = 44.9, c = 38.0 A, and beta = 94.0 degrees, P2(1)2(1)2(1) with a = 44.3, b = 63.7 and c = 72.7 A, and a tetragonal form P4(1)2(1)2 with a = b = 58.6 and c = 151.8 A. The structures of all three crystals have been solved by molecular replacement and subsequently refined to R factors of 0.184 for the monoclinic at 2.6 A, 0.165 for the orthorhombic at 1.75 A, and 0.181 for the tetragonal, also at 1.75 A resolution. No solvent was included in the monoclinic crystal while 123 and 105 water molecules were included in the higher resolution orthorhombic and tetragonal structures, respectively. A bound tartrate molecule was also clearly visible in the tetragonal structure. The r.m.s. deviations between molecular structures in the three crystals range from 0.6 to 0.7 A for Calpha atoms, and 1.1 to 1.3 A for all atoms. This is comparable to the r.m.s. deviation between the three structures and the starting model. Nevertheless, several peptide loops show particularly large variations from the initial model.
About this Structure
1THW is a Single protein structure of sequence from Thaumatococcus daniellii with as ligand. Full crystallographic information is available from OCA.
Reference
Structures of three crystal forms of the sweet protein thaumatin., Ko TP, Day J, Greenwood A, McPherson A, Acta Crystallogr D Biol Crystallogr. 1994 Nov 1;50(Pt 6):813-25. PMID:15299348
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