5t3g: Difference between revisions

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'''Unreleased structure'''


The entry 5t3g is ON HOLD  until Paper Publication
==thaumatin soaked with selenourea for 10 min==
<StructureSection load='5t3g' size='340' side='right' caption='[[5t3g]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5t3g]] 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=5T3G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T3G FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEY:SELENOUREA'>SEY</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">[[5t3f|5t3f]]</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5t3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t3g OCA], [http://pdbe.org/5t3g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t3g RCSB], [http://www.ebi.ac.uk/pdbsum/5t3g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t3g ProSAT]</span></td></tr>
</table>
== Function ==
[[http://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 ==
Majority of novel X-ray crystal structures of proteins are currently solved using the anomalous diffraction signal provided by selenium after incorporation of selenomethionine instead of natural methionine by genetic engineering methods. However, selenium can be inserted into protein crystals in the form of selenourea (SeC(NH2)2), by adding the crystalline powder of selenourea into mother liquor or cryo-solution with native crystals, in analogy to the classic procedure of heavy-atom derivatization. Selenourea is able to bind to reactive groups at the surface of macromolecules primarily through hydrogen bonds, where the selenium atom may serve as acceptor and amide groups as donors. Selenourea has different chemical properties than heavy-atom reagents and halide ions and provides a convenient way of phasing crystal structures of macromolecules.


Authors: Luo, Z., Dauter, Z.
Selenourea: a convenient phasing vehicle for macromolecular X-ray crystal structures.,Luo Z Sci Rep. 2016 Nov 14;6:37123. doi: 10.1038/srep37123. PMID:27841370<ref>PMID:27841370</ref>


Description: thaumatin soaked with selenourea for 10 min
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5t3g" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Thaumatococcus daniellii]]
[[Category: Dauter, Z]]
[[Category: Dauter, Z]]
[[Category: Luo, Z]]
[[Category: Luo, Z]]
[[Category: Plant protein]]
[[Category: Selenourea]]
[[Category: Thaumatin]]
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