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New page: left|200px<br /><applet load="1ly0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ly0, resolution 1.36Å" /> '''Structure of thaumat... |
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== | ==Structure of thaumatin crystallized in the presence of glycerol== | ||
The intensely sweet protein thaumatin has been crystallized at 293 K in | <StructureSection load='1ly0' size='340' side='right'caption='[[1ly0]], [[Resolution|resolution]] 1.36Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1ly0]] 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=1LY0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LY0 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]] 1.36Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></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=1ly0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ly0 OCA], [https://pdbe.org/1ly0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ly0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ly0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ly0 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/ly/1ly0_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=1ly0 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The intensely sweet protein thaumatin has been crystallized at 293 K in the presence of sodium tartrate and 25%(v/v) glycerol for X-ray diffraction data collection at 100 K. A comparison of the three-dimensional structure model derived from a crystal grown in the presence of glycerol with that of a control deprived of this additive reveals only minor changes in the overall structure but a approximately 20% reduction in the number of water molecules. X-ray topography analyses show that the overall quality of the crystals prepared in the presence of this cryoprotectant is enhanced. | |||
Crystallization in the presence of glycerol displaces water molecules in the structure of thaumatin.,Charron C, Kadri A, Robert MC, Giege R, Lorber B Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):2060-5. Epub 2002, Nov 23. PMID:12454465<ref>PMID:12454465</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 1ly0" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thaumatococcus daniellii]] | [[Category: Thaumatococcus daniellii]] | ||
[[Category: Charron | [[Category: Charron C]] | ||
[[Category: Giege | [[Category: Giege R]] | ||
[[Category: Kadri | [[Category: Kadri A]] | ||
[[Category: Lorber | [[Category: Lorber B]] | ||
[[Category: Robert | [[Category: Robert MC]] | ||
Latest revision as of 03:13, 21 November 2024
Structure of thaumatin crystallized in the presence of glycerolStructure of thaumatin crystallized in the presence of glycerol
Structural highlights
FunctionTHM1_THADA Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe intensely sweet protein thaumatin has been crystallized at 293 K in the presence of sodium tartrate and 25%(v/v) glycerol for X-ray diffraction data collection at 100 K. A comparison of the three-dimensional structure model derived from a crystal grown in the presence of glycerol with that of a control deprived of this additive reveals only minor changes in the overall structure but a approximately 20% reduction in the number of water molecules. X-ray topography analyses show that the overall quality of the crystals prepared in the presence of this cryoprotectant is enhanced. Crystallization in the presence of glycerol displaces water molecules in the structure of thaumatin.,Charron C, Kadri A, Robert MC, Giege R, Lorber B Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):2060-5. Epub 2002, Nov 23. PMID:12454465[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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