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| | ==Crystal Structure of The Recombinant Thaumatin II at 0.99 A== | | ==Crystal Structure of The Recombinant Thaumatin II at 0.99 A== |
| - | <StructureSection load='3wou' size='340' side='right' caption='[[3wou]], [[Resolution|resolution]] 0.99Å' scene=''> | + | <StructureSection load='3wou' size='340' side='right'caption='[[3wou]], [[Resolution|resolution]] 0.99Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wou]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Katemfe Katemfe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WOU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WOU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wou]] 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=3WOU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WOU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</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]] 0.99Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3aok|3aok]], [[3al7|3al7]], [[3ald|3ald]], [[3vhg|3vhg]], [[3vhf|3vhf]], [[3vjq|3vjq]], [[3wox|3wox]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wou OCA], [http://pdbe.org/3wou PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wou RCSB], [http://www.ebi.ac.uk/pdbsum/3wou PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wou 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=3wou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wou OCA], [https://pdbe.org/3wou PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wou RCSB], [https://www.ebi.ac.uk/pdbsum/3wou PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wou ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/THM2_THADA THM2_THADA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Katemfe]] | + | [[Category: Large Structures]] |
| - | [[Category: Masuda, T]] | + | [[Category: Thaumatococcus daniellii]] |
| - | [[Category: Mikami, B]] | + | [[Category: Masuda T]] |
| - | [[Category: Tani, F]] | + | [[Category: Mikami B]] |
| - | [[Category: Osmotin]] | + | [[Category: Tani F]] |
| - | [[Category: Plant protein]]
| + | |
| - | [[Category: Sweet receptor]]
| + | |
| - | [[Category: Sweet-tasting protein]]
| + | |
| - | [[Category: Thaumatin-like protein]]
| + | |
| Structural highlights
Function
THM2_THADA
Publication Abstract from PubMed
Thaumatin, an intensely sweet-tasting protein used as a sweetener, elicits a sweet taste at 50 nM. Although two major variants designated thaumatin I and thaumatin II exist in plants, there have been few dedicated thaumatin II structural studies and, to date, data beyond atomic resolution had not been obtained. To identify the detailed structural properties explaining why thaumatin elicits a sweet taste, the structure of recombinant thaumatin II was determined at the resolution of 0.99 A. Atomic resolution structural analysis with riding hydrogen atoms illustrated the differences in the direction of the side-chains more precisely and the electron density maps of the C-terminal regions were markedly improved. Though it had been suggested that the three consecutive glycine residues (G142-G143-G144) have highly flexible conformations, G143, the central glycine residue was successfully modelled in two conformations for the first time. Furthermore, the side chain r.m.s.d. values for two residues (R67 and R82) critical for sweetness exhibited substantially higher values, suggesting that these residues are highly disordered. These results demonstrated that the flexible conformations in two critical residues favoring their interaction with sweet taste receptors are prominent features of the intensely sweet taste of thaumatin.
Atomic structure of recombinant thaumatin II reveals flexible conformations in two residues critical for sweetness and three consecutive glycine residues.,Masuda T, Mikami B, Tani F Biochimie. 2014 Jul 24. pii: S0300-9084(14)00207-7. doi:, 10.1016/j.biochi.2014.07.016. PMID:25066915[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Masuda T, Mikami B, Tani F. Atomic structure of recombinant thaumatin II reveals flexible conformations in two residues critical for sweetness and three consecutive glycine residues. Biochimie. 2014 Jul 24. pii: S0300-9084(14)00207-7. doi:, 10.1016/j.biochi.2014.07.016. PMID:25066915 doi:http://dx.doi.org/10.1016/j.biochi.2014.07.016
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