6rek: Difference between revisions
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==Crystal structure of Pizza6-SH with Cu2+== | |||
<StructureSection load='6rek' size='340' side='right'caption='[[6rek]], [[Resolution|resolution]] 1.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6rek]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6REK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6REK 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]] 1.1Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=6rek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rek OCA], [https://pdbe.org/6rek PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rek RCSB], [https://www.ebi.ac.uk/pdbsum/6rek PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rek ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We developed an artificial hydrolase based on the symmetrical Pizza6 beta-propeller protein for the metal-free hydrolysis of 4-nitrophenyl acetate and butyrate. Through site-specific mutagenesis and crystallisation studies, the catalytic mechanism was investigated and found to be dependent on a threonine-histidine dyad. The mutant with additional histidine residues generated the highest kcat values, forming a His-His-Thr triad and matched previously reported metalloenzymes. The highly symmetrical beta-propeller artificial enzymes and their protein-metal complexes have potential to be utilised in bioinorganic and supramolecular chemistry, as well as being developed further into 2D/3D catalytic materials. | |||
Artificial beta-propeller protein-based hydrolases.,Clarke DE, Noguchi H, Gryspeerdt JAG, De Feyter S, Voet ARD Chem Commun (Camb). 2019 Jul 23;55(60):8880-8883. doi: 10.1039/c9cc04388h. PMID:31321399<ref>PMID:31321399</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6rek" style="background-color:#fffaf0;"></div> | ||
[[Category: Clarke | == References == | ||
[[Category: | <references/> | ||
[[Category: Gryspeerdt | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Synthetic construct]] | |||
[[Category: Clarke DE]] | |||
[[Category: Feyter SD]] | |||
[[Category: Gryspeerdt JL]] | |||
[[Category: Noguchi H]] | |||
[[Category: Voet ARD]] | |||