5wbb: Difference between revisions
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The | ==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]] | |||
