5avg: Difference between revisions
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The | ==The 0.95 angstrom structure of thaumatin crystallized in high-strength agarose hydrogel== | ||
<StructureSection load='5avg' size='340' side='right'caption='[[5avg]], [[Resolution|resolution]] 0.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5avg]] 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=5AVG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AVG FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.95Å</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=5avg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5avg OCA], [https://pdbe.org/5avg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5avg RCSB], [https://www.ebi.ac.uk/pdbsum/5avg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5avg ProSAT]</span></td></tr> | |||
</table> | |||
== 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;"> | |||
== Publication Abstract from PubMed == | |||
High-throughput protein X-ray crystallography offers a significant opportunity to facilitate drug discovery. The most reliable approach is to determine the three-dimensional structure of the protein-ligand complex by soaking the ligand in apo crystals. However, protein apo crystals produced by conventional crystallization in a solution are fatally damaged by osmotic shock during soaking. To overcome this difficulty, we present a novel technique for growing protein crystals in a high-concentration hydrogel that is completely gellified and exhibits high strength. This technique allowed us essentially to increase the mechanical stability of the crystals, preventing serious damage to the crystals caused by osmotic shock. Thus, this method may accelerate structure-based drug discoveries. | |||
Growth of protein crystals in hydrogels prevents osmotic shock.,Sugiyama S, Maruyama M, Sazaki G, Hirose M, Adachi H, Takano K, Murakami S, Inoue T, Mori Y, Matsumura H J Am Chem Soc. 2012 Apr 4;134(13):5786-9. doi: 10.1021/ja301584y. Epub 2012 Mar, 27. PMID:22435400<ref>PMID:22435400</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5avg" style="background-color:#fffaf0;"></div> | ||
[[Category: Hirose | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: Matsumura | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Murakami | [[Category: Thaumatococcus daniellii]] | ||
[[Category: | [[Category: Adachi H]] | ||
[[Category: | [[Category: Hirose M]] | ||
[[Category: | [[Category: Inoue T]] | ||
[[Category: | [[Category: Maruyama M]] | ||
[[Category: Matsumura H]] | |||
[[Category: Mori Y]] | |||
[[Category: Murakami S]] | |||
[[Category: Sazaki G]] | |||
[[Category: Shimizu N]] | |||
[[Category: Sugiyama S]] | |||
[[Category: Takano K]] | |||
Latest revision as of 18:49, 8 November 2023
The 0.95 angstrom structure of thaumatin crystallized in high-strength agarose hydrogelThe 0.95 angstrom structure of thaumatin crystallized in high-strength agarose hydrogel
Structural highlights
FunctionTHM1_THADA Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis. Publication Abstract from PubMedHigh-throughput protein X-ray crystallography offers a significant opportunity to facilitate drug discovery. The most reliable approach is to determine the three-dimensional structure of the protein-ligand complex by soaking the ligand in apo crystals. However, protein apo crystals produced by conventional crystallization in a solution are fatally damaged by osmotic shock during soaking. To overcome this difficulty, we present a novel technique for growing protein crystals in a high-concentration hydrogel that is completely gellified and exhibits high strength. This technique allowed us essentially to increase the mechanical stability of the crystals, preventing serious damage to the crystals caused by osmotic shock. Thus, this method may accelerate structure-based drug discoveries. Growth of protein crystals in hydrogels prevents osmotic shock.,Sugiyama S, Maruyama M, Sazaki G, Hirose M, Adachi H, Takano K, Murakami S, Inoue T, Mori Y, Matsumura H J Am Chem Soc. 2012 Apr 4;134(13):5786-9. doi: 10.1021/ja301584y. Epub 2012 Mar, 27. PMID:22435400[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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