6gmi
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Genetic Engineering of an Artificial Metalloenzyme for Transfer Hydrogenation of a Self-Immolative Substrate in E. coli's Periplasm.== | |
| + | <StructureSection load='6gmi' size='340' side='right' caption='[[6gmi]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6gmi]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GMI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GMI FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4IR:{N-(4-{[2-(AMINO-KAPPAN)ETHYL]SULFAMOYL-KAPPAN}PHENYL)-5-[(3AS,4S,6AR)-2-OXOHEXAHYDRO-1H-THIENO[3,4-D]IMIDAZOL-4-YL]PENTANAMIDE}(CHLORO)[(1,2,3,4,5-ETA)-1,2,3,4,5-PENTAMETHYLCYCLOPENTADIENYL]IRIDIUM(III)'>4IR</scene>, <scene name='pdbligand=IR3:IRIDIUM+(III)+ION'>IR3</scene></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=6gmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gmi OCA], [http://pdbe.org/6gmi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gmi RCSB], [http://www.ebi.ac.uk/pdbsum/6gmi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gmi ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/SAV_STRAV SAV_STRAV]] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Artificial metalloenzymes (ArMs), which combine an abiotic metal cofactor with a protein scaffold, catalyze various synthetically useful transformations. To complement the natural enzymes' repertoire, effective optimization protocols to improve ArM's performance are required. Here we report on our efforts to optimize the activity of an artificial transfer hydrogenase (ATHase) using Escherichia coli whole cells. For this purpose, we rely on a self-immolative quinolinium substrate which, upon reduction, releases fluorescent umbelliferone, thus allowing efficient screening. Introduction of a loop in the immediate proximity of the Ir-cofactor afforded an ArM with up to 5-fold increase in transfer hydrogenation activity compared to the wild-type ATHase using purified mutants. | ||
| - | + | Genetic Engineering of an Artificial Metalloenzyme for Transfer Hydrogenation of a Self-Immolative Substrate in Escherichia coli's Periplasm.,Zhao J, Rebelein JG, Mallin H, Trindler C, Pellizzoni MM, Ward TR J Am Chem Soc. 2018 Oct 3. doi: 10.1021/jacs.8b07189. PMID:30272972<ref>PMID:30272972</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6gmi" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Rebelein, J G]] | ||
| + | [[Category: Artificial transfer hydrogenase]] | ||
| + | [[Category: Beta barrel]] | ||
| + | [[Category: Biotin-binding protein]] | ||
| + | [[Category: Streptavidin]] | ||
Revision as of 08:14, 10 October 2018
Genetic Engineering of an Artificial Metalloenzyme for Transfer Hydrogenation of a Self-Immolative Substrate in E. coli's Periplasm.
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