5ln0: Difference between revisions
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<StructureSection load='5ln0' size='340' side='right'caption='[[5ln0]], [[Resolution|resolution]] 1.95Å' scene=''> | <StructureSection load='5ln0' size='340' side='right'caption='[[5ln0]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ln0]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5ln0]] 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=5LN0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LN0 FirstGlance]. <br> | ||
</td></tr><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> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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=5ln0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ln0 OCA], [https://pdbe.org/5ln0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ln0 RCSB], [https://www.ebi.ac.uk/pdbsum/5ln0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ln0 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: Betzel | [[Category: Betzel C]] | ||
[[Category: Bourenkov | [[Category: Bourenkov G]] | ||
[[Category: Giquel | [[Category: Giquel Y]] | ||
[[Category: Heymann | [[Category: Heymann M]] | ||
[[Category: Kapis | [[Category: Kapis S]] | ||
[[Category: Perbandt | [[Category: Perbandt M]] | ||
[[Category: Schneider | [[Category: Schneider T]] | ||
[[Category: Schubert | [[Category: Schubert R]] | ||
Latest revision as of 21:35, 18 October 2023
Low dose Thaumatin - 760-800 ms.Low dose Thaumatin - 760-800 ms.
Structural highlights
FunctionTHM1_THADA Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis. Publication Abstract from PubMedMany biochemical processes take place on timescales ranging from femto-seconds to seconds. Accordingly, any time-resolved experiment must be matched to the speed of the structural changes of interest. Therefore, the timescale of interest defines the requirements of the X-ray source, instrumentation and data-collection strategy. In this study, a minimalistic approach for in situ crystallization is presented that requires only a few microlitres of sample solution containing a few hundred crystals. It is demonstrated that complete diffraction data sets, merged from multiple crystals, can be recorded within only a few minutes of beamtime and allow high-resolution structural information of high quality to be obtained with a temporal resolution of 40 ms. Global and site-specific radiation damage can be avoided by limiting the maximal dose per crystal to 400 kGy. Moreover, analysis of the data collected at higher doses allows the time-resolved observation of site-specific radiation damage. Therefore, our approach is well suited to observe structural changes and possibly enzymatic reactions in the low-millisecond regime. A multicrystal diffraction data-collection approach for studying structural dynamics with millisecond temporal resolution.,Schubert R, Kapis S, Gicquel Y, Bourenkov G, Schneider TR, Heymann M, Betzel C, Perbandt M IUCrJ. 2016 Oct 26;3(Pt 6):393-401. eCollection 2016 Nov 1. PMID:27840678[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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