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| | <StructureSection load='2g4y' size='340' side='right'caption='[[2g4y]], [[Resolution|resolution]] 1.98Å' scene=''> | | <StructureSection load='2g4y' size='340' side='right'caption='[[2g4y]], [[Resolution|resolution]] 1.98Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2g4y]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G4Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2G4Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2g4y]] 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=2G4Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G4Y FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.98Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2g4h|2g4h]], [[2g4i|2g4i]], [[2g4j|2g4j]], [[2g4k|2g4k]], [[2g4l|2g4l]], [[2g4m|2g4m]], [[2g4n|2g4n]], [[2g4o|2g4o]], [[2g4p|2g4p]], [[2g4q|2g4q]], [[2g4r|2g4r]], [[2g4s|2g4s]], [[2g4t|2g4t]], [[2g4u|2g4u]], [[2g4v|2g4v]], [[2g4w|2g4w]], [[2g4x|2g4x]], [[2g4z|2g4z]], [[2g51|2g51]], [[2g52|2g52]], [[2g55|2g55]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2g4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g4y OCA], [http://pdbe.org/2g4y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2g4y RCSB], [http://www.ebi.ac.uk/pdbsum/2g4y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2g4y ProSAT]</span></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=2g4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g4y OCA], [https://pdbe.org/2g4y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g4y RCSB], [https://www.ebi.ac.uk/pdbsum/2g4y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g4y ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g4/2g4y_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g4/2g4y_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Thaumatococcus daniellii]] | | [[Category: Thaumatococcus daniellii]] |
| - | [[Category: Mueller-Dieckmann, C]] | + | [[Category: Mueller-Dieckmann C]] |
| - | [[Category: Weiss, M S]] | + | [[Category: Weiss MS]] |
| - | [[Category: Plant protein]]
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| - | [[Category: Thaumatin structure at a wavelength of 2 some]]
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| Structural highlights
Function
THM1_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 PubMed
23 different crystal forms of 19 different biological macromolecules were examined with respect to their anomalously scattering substructures using diffraction data collected at a wavelength of 2.0 A (6.2 keV). In more than 90% of the cases the substructure was found to contain more than just the protein S atoms. The data presented suggest that chloride, sulfate, phosphate or metal ions from the buffer or even from the purification protocol are frequently bound to the protein molecule and that these ions are often overlooked, especially if they are not bound at full occupancy. Thus, in order to fully describe the macromolecule under study, it seems desirable that any structure determination be complemented with a long-wavelength data set.
On the routine use of soft X-rays in macromolecular crystallography. Part IV. Efficient determination of anomalous substructures in biomacromolecules using longer X-ray wavelengths.,Mueller-Dieckmann C, Panjikar S, Schmidt A, Mueller S, Kuper J, Geerlof A, Wilmanns M, Singh RK, Tucker PA, Weiss MS Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):366-80. Epub 2007, Feb 21. PMID:17327674[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mueller-Dieckmann C, Panjikar S, Schmidt A, Mueller S, Kuper J, Geerlof A, Wilmanns M, Singh RK, Tucker PA, Weiss MS. On the routine use of soft X-rays in macromolecular crystallography. Part IV. Efficient determination of anomalous substructures in biomacromolecules using longer X-ray wavelengths. Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):366-80. Epub 2007, Feb 21. PMID:17327674 doi:http://dx.doi.org/10.1107/S0907444906055624
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