6l2e: Difference between revisions

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'''Unreleased structure'''


The entry 6l2e is ON HOLD
==Crystal structure of a cupin protein (tm1459, H52A mutant) in copper (Cu) substituted form==
<StructureSection load='6l2e' size='340' side='right'caption='[[6l2e]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6l2e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L2E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L2E 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]] 1.201&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</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=6l2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l2e OCA], [https://pdbe.org/6l2e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l2e RCSB], [https://www.ebi.ac.uk/pdbsum/6l2e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l2e ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9X1H0_THEMA Q9X1H0_THEMA]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cupin superfamily proteins (TM1459) work as a macromolecular ligand framework with a double-stranded beta-barrel structure ligating to a Cu ion through histidine side chains. Variegating the first coordination sphere of TM1459 revealed that H52A and H54A/H58A mutants effectively catalyzed the diastereo- and enantioselective Michael addition reaction of nitroalkanes to an alpha,beta-unsaturated ketone. Moreover, calculated substrate docking signified C106N and F104W single-point mutations, which inverted the diastereoselectivity of H52A and further improved the stereoselectivity of H54A/H58A, respectively.


Authors: Fujieda, N., Ichihashi, H., Nishikawa, Y., Kurisu, G., Itoh, S.
Cupin Variants as a Macromolecular Ligand Library for Stereoselective Michael Addition of Nitroalkanes.,Fujieda N, Ichihashi H, Yuasa M, Nishikawa Y, Kurisu G, Itoh S Angew Chem Int Ed Engl. 2020 Feb 19. doi: 10.1002/anie.202000129. PMID:32073197<ref>PMID:32073197</ref>


Description: Crystal structure of a cupin protein (tm1459, H52A mutant) in copper (Cu) substituted form
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Kurisu, G]]
<div class="pdbe-citations 6l2e" style="background-color:#fffaf0;"></div>
[[Category: Itoh, S]]
== References ==
[[Category: Ichihashi, H]]
<references/>
[[Category: Nishikawa, Y]]
__TOC__
[[Category: Fujieda, N]]
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermotoga maritima MSB8]]
[[Category: Fujieda N]]
[[Category: Ichihashi H]]
[[Category: Itoh S]]
[[Category: Kurisu G]]
[[Category: Nishikawa Y]]
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