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New page: left|200px<br /><applet load="1thu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1thu, resolution 2.6Å" /> '''THE STRUCTURES OF THR...
 
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[[Image:1thu.gif|left|200px]]<br /><applet load="1thu" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1thu, resolution 2.6&Aring;" />
'''THE STRUCTURES OF THREE CRYSTAL FORMS OF THE SWEET PROTEIN THAUMATIN'''<br />


==Overview==
==THE STRUCTURES OF THREE CRYSTAL FORMS OF THE SWEET PROTEIN THAUMATIN==
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.
<StructureSection load='1thu' size='340' side='right'caption='[[1thu]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1thu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1THU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1THU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1thu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1thu OCA], [https://pdbe.org/1thu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1thu RCSB], [https://www.ebi.ac.uk/pdbsum/1thu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1thu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/THM1_THADA THM1_THADA] Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/th/1thu_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1thu ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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==
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<ref>PMID:15299348</ref>
1THU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1THU OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299348 15299348]
</div>
[[Category: Single protein]]
<div class="pdbe-citations 1thu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thaumatococcus daniellii]]
[[Category: Thaumatococcus daniellii]]
[[Category: Day, J.]]
[[Category: Day J]]
[[Category: Greenwood, A.]]
[[Category: Greenwood A]]
[[Category: Ko, T.P.]]
[[Category: Ko T-P]]
[[Category: McPherson, A.]]
[[Category: McPherson A]]
[[Category: sweet tasting protein]]
 
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