6coa: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6coa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1kwn 1kwn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6COA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6COA FirstGlance]. <br> | <table><tr><td colspan='2'>[[6coa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1kwn 1kwn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6COA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6COA FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2Å</td></tr> | ||
<tr id=' | <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=6coa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6coa OCA], [https://pdbe.org/6coa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6coa RCSB], [https://www.ebi.ac.uk/pdbsum/6coa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6coa 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=6coa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6coa OCA], [https://pdbe.org/6coa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6coa RCSB], [https://www.ebi.ac.uk/pdbsum/6coa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6coa ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Thaumatococcus daniellii]] | [[Category: Thaumatococcus daniellii]] | ||
[[Category: Brzezinski | [[Category: Brzezinski D]] | ||
[[Category: Giege | [[Category: Giege R]] | ||
[[Category: Lorber | [[Category: Lorber B]] | ||
[[Category: Porebski | [[Category: Porebski PJ]] | ||
[[Category: Sauter | [[Category: Sauter C]] | ||
[[Category: Shabalin | [[Category: Shabalin IG]] | ||
Latest revision as of 18:08, 4 October 2023
1.2 A Structure of Thaumatin Crystallized in Gel1.2 A Structure of Thaumatin Crystallized in Gel
Structural highlights
FunctionTHM1_THADA Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis. Publication Abstract from PubMedOne reason for introducing a gel in the crystallization medium of proteins is its ability to reduce convection in solution. This can lead to better nucleation and growth conditions, and to crystals having enhanced diffraction properties. We report here the X-ray characterization at room temperature of high-quality crystals of the intensely sweet thaumatin prepared in a sodium tartrate solution gelified with 0.15% (m/v) agarose. Using a synchrotron radiation, these crystals diffracted to a previously unachieved resolution. A diffraction dataset was collected from four crystals at a resolution of 1.2 A with a R(sym) of 3.6% and a completeness of 99%. Refinement was carried out to a final crystallographic R-factor of 12.0%. The quality of the electron density map allowed for the observation of fine structural details in the protein and its solvation shell. Crystallization in gel might be used more generally to improve the quality of macromolecular crystals. Advantages provided by the gelified medium in the frame of structural studies are emphasized. Towards atomic resolution with crystals grown in gel: the case of thaumatin seen at room temperature.,Sauter C, Lorber B, Giege R Proteins. 2002 Aug 1;48(2):146-50. PMID:12112683[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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