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5wbb
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Peroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins - S112A== | |
| + | <StructureSection load='5wbb' size='340' side='right' caption='[[5wbb]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5wbb]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WBB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WBB FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=SQ1:[N-(2-{bis[2-(pyridin-2-yl-kappaN)ethyl]amino-kappaN}ethyl)-5-(2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanamide]copper'>SQ1</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=5wbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wbb OCA], [http://pdbe.org/5wbb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wbb RCSB], [http://www.ebi.ac.uk/pdbsum/5wbb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wbb 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 == | ||
| + | Copper-hydroperoxido species (CuII-OOH) have been proposed to be key intermediates in biological and synthetic oxidations. Using biotin-streptavidin (Sav) technology, artificial copper proteins have been developed to stabilize a CuII-OOH complex in solution and in crystallo. Stability is achieved because the Sav host provides a local environment around the Cu-OOH that includes a network of hydrogen bonds to the hydroperoxido ligand. Systematic deletions of individual hydrogen bonds to the Cu-OOH complex were accomplished using different Sav variants and demonstrated that stability is achieved with a single hydrogen bond to the proximal O-atom of the hydroperoxido ligand: changing this interaction to only include the distal O-atom produced a reactive variant that oxidized an external substrate. | ||
| - | + | Peroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins.,Mann SI, Heinisch T, Ward TR, Borovik AS J Am Chem Soc. 2017 Nov 15. doi: 10.1021/jacs.7b10452. PMID:29117678<ref>PMID:29117678</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: Borovik, A | + | <div class="pdbe-citations 5wbb" style="background-color:#fffaf0;"></div> |
| - | + | == References == | |
| - | + | <references/> | |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Borovik, A S]] | ||
[[Category: Heinisch, T]] | [[Category: Heinisch, T]] | ||
| + | [[Category: Mann, S I]] | ||
| + | [[Category: Ward, T R]] | ||
| + | [[Category: Biotin]] | ||
| + | [[Category: Biotin binding protein]] | ||
| + | [[Category: Copper]] | ||
| + | [[Category: Hydrogen bond]] | ||
| + | [[Category: Hydroperoxo]] | ||
| + | [[Category: Metal binding protein]] | ||
| + | [[Category: Secondary coordination sphere]] | ||
| + | [[Category: Streptavidin]] | ||
Revision as of 07:44, 22 November 2017
Peroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins - S112A
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