3vjq: Difference between revisions
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[[ | ==Recombinant thaumatin at pH 8.0 with hydrogen atoms== | ||
<StructureSection load='3vjq' size='340' side='right' caption='[[3vjq]], [[Resolution|resolution]] 1.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3vjq]] 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=3VJQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VJQ FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3al7|3al7]], [[3ald|3ald]], [[3aok|3aok]], [[3vhf|3vhf]], [[3vhg|3vhg]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vjq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vjq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vjq RCSB], [http://www.ebi.ac.uk/pdbsum/3vjq PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Thaumatin, an intensely sweet-tasting plant protein, elicits a sweet taste at 50 nM. Although the sweetness remains when thaumatin is heated at 80 degrees C for 4h under acid conditions, it rapidly declines when heating at a pH above 6.5. To clarify the structural difference at high pH, the atomic structure of a recombinant thaumatin I at pH 8.0 was determined at a resolution of 1.0A. Comparison to the crystal structure of thaumatin at pH 7.3 and 7.0 revealed the root-mean square deviation value of a Calpha atom to be substantially greater in the large disulfide-rich region of domain II, especially residues 154-164, suggesting that a loop region in domain II to be affected by solvent conditions. Furthermore, B-factors of Lys137, Lys163, and Lys187 were significantly affected by pH change, suggesting that a striking increase in the mobility of these lysine residues, which could facilitate a reaction with a free sulfhydryl residue produced via the beta-elimination of disulfide bonds by heating at a pH above 7.0. The increase in mobility of lysine residues as well as a loop region in domain II might play an important role in the heat-induced aggregation of thaumatin above pH 7.0. | |||
Atomic structure of the sweet-tasting protein thaumatin I at pH 8.0 reveals the large disulfide-rich region in domain II to be sensitive to a pH change.,Masuda T, Ohta K, Mikami B, Kitabatake N, Tani F Biochem Biophys Res Commun. 2012 Mar 2;419(1):72-6. Epub 2012 Feb 3. PMID:22326916<ref>PMID:22326916</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Thaumatococcus daniellii]] | [[Category: Thaumatococcus daniellii]] | ||
[[Category: Masuda, T.]] | [[Category: Masuda, T.]] | ||
Revision as of 10:41, 5 June 2014
Recombinant thaumatin at pH 8.0 with hydrogen atomsRecombinant thaumatin at pH 8.0 with hydrogen atoms
Structural highlights
Publication Abstract from PubMedThaumatin, an intensely sweet-tasting plant protein, elicits a sweet taste at 50 nM. Although the sweetness remains when thaumatin is heated at 80 degrees C for 4h under acid conditions, it rapidly declines when heating at a pH above 6.5. To clarify the structural difference at high pH, the atomic structure of a recombinant thaumatin I at pH 8.0 was determined at a resolution of 1.0A. Comparison to the crystal structure of thaumatin at pH 7.3 and 7.0 revealed the root-mean square deviation value of a Calpha atom to be substantially greater in the large disulfide-rich region of domain II, especially residues 154-164, suggesting that a loop region in domain II to be affected by solvent conditions. Furthermore, B-factors of Lys137, Lys163, and Lys187 were significantly affected by pH change, suggesting that a striking increase in the mobility of these lysine residues, which could facilitate a reaction with a free sulfhydryl residue produced via the beta-elimination of disulfide bonds by heating at a pH above 7.0. The increase in mobility of lysine residues as well as a loop region in domain II might play an important role in the heat-induced aggregation of thaumatin above pH 7.0. Atomic structure of the sweet-tasting protein thaumatin I at pH 8.0 reveals the large disulfide-rich region in domain II to be sensitive to a pH change.,Masuda T, Ohta K, Mikami B, Kitabatake N, Tani F Biochem Biophys Res Commun. 2012 Mar 2;419(1):72-6. Epub 2012 Feb 3. PMID:22326916[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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