4ekt: Difference between revisions
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==Final Thaumatin Structure for Radiation Damage Experiment at 180 K== | ==Final Thaumatin Structure for Radiation Damage Experiment at 180 K== | ||
<StructureSection load='4ekt' size='340' side='right' caption='[[4ekt]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='4ekt' size='340' side='right'caption='[[4ekt]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ekt]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ekt]] 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=4EKT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EKT 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]] 1.75Å</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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ekt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ekt OCA], [https://pdbe.org/4ekt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ekt RCSB], [https://www.ebi.ac.uk/pdbsum/4ekt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ekt 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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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4ekt" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Thaumatococcus daniellii]] | [[Category: Thaumatococcus daniellii]] | ||
[[Category: Badeau | [[Category: Badeau R]] | ||
[[Category: Hopkins | [[Category: Hopkins JB]] | ||
[[Category: Thorne | [[Category: Thorne RE]] | ||
[[Category: Warkentin | [[Category: Warkentin M]] | ||
Latest revision as of 05:50, 21 November 2024
Final Thaumatin Structure for Radiation Damage Experiment at 180 KFinal Thaumatin Structure for Radiation Damage Experiment at 180 K
Structural highlights
FunctionTHM1_THADA Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis. Publication Abstract from PubMedThe spatial distribution of radiation damage (assayed by increases in atomic B factors) to thaumatin and urease crystals at temperatures ranging from 25 to 300 K is reported. The nature of the damage changes dramatically at approximately 180 K. Above this temperature the role of solvent diffusion is apparent in thaumatin crystals, as solvent-exposed turns and loops are especially sensitive. In urease, a flap covering the active site is the most sensitive part of the molecule and nearby loops show enhanced sensitivity. Below 180 K sensitivity is correlated with poor local packing, especially in thaumatin. At all temperatures, the component of the damage that is spatially uniform within the unit cell accounts for more than half of the total increase in the atomic B factors and correlates with changes in mosaicity. This component may arise from lattice-level, rather than local, disorder. The effects of primary structure on radiation sensitivity are small compared with those of tertiary structure, local packing, solvent accessibility and crystal contacts. Spatial distribution of radiation damage to crystalline proteins at 25-300 K.,Warkentin M, Badeau R, Hopkins JB, Thorne RE Acta Crystallogr D Biol Crystallogr. 2012 Sep;68(Pt 9):1108-17. doi:, 10.1107/S0907444912021361. Epub 2012 Aug 18. PMID:22948911[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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