3ald: Difference between revisions

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<StructureSection load='3ald' size='340' side='right'caption='[[3ald]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
<StructureSection load='3ald' size='340' side='right'caption='[[3ald]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ald]] 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=3ALD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3ALD FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ald]] 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=3ALD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ALD FirstGlance]. <br>
</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>
</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3al7|3al7]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3al7|3al7]]</div></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3ald FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ald OCA], [http://pdbe.org/3ald PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ald RCSB], [http://www.ebi.ac.uk/pdbsum/3ald PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ald 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=3ald FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ald OCA], [https://pdbe.org/3ald PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ald RCSB], [https://www.ebi.ac.uk/pdbsum/3ald PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ald ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">

Revision as of 16:26, 4 May 2022

Crystal structure of sweet-tasting protein Thaumatin I at 1.10 ACrystal structure of sweet-tasting protein Thaumatin I at 1.10 A

Structural highlights

3ald is a 1 chain structure with sequence from Thaumatococcus daniellii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Thaumatin, an intensely sweet-tasting plant protein, elicits a sweet taste at a concentration of 50 nM. The crystal structure of a recombinant form of thaumatin I produced in the yeast Pichia pastoris has been determined to a resolution of 1.1 A. The model was refined with anisotropic B parameters and riding H atoms. A comparison of the diffraction data and refinement statistics for recombinant thaumatin I with those for plant thaumatin I revealed no significant differences in the diffraction data. The R values for recombinant thaumatin I and plant thaumatin I (F(o) > 4sigma) were 9.11% and 9.91%, respectively, indicating the final model to be of good quality. Notably, the electron-density maps around Asn46 and Ser63, which differ between thaumatin variants, were significantly improved. Furthermore, a number of H atoms became visible in an OMIT map and could be assigned. The high-quality structure of recombinant thaumatin with H atoms should provide details about sweetness determinants in thaumatin and provide valuable insights into the mechanism of its interaction with taste receptors.

High-resolution structure of the recombinant sweet-tasting protein thaumatin I.,Masuda T, Ohta K, Mikami B, Kitabatake N Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jun 1;67(Pt, 6):652-8. Epub 2011 May 24. PMID:21636903[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Masuda T, Ohta K, Mikami B, Kitabatake N. High-resolution structure of the recombinant sweet-tasting protein thaumatin I. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jun 1;67(Pt, 6):652-8. Epub 2011 May 24. PMID:21636903 doi:10.1107/S174430911101373X

3ald, resolution 1.10Å

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