View source for 6vjk


==Streptavidin mutant M88 (N49C/A86C)==
<StructureSection load='6vjk' size='340' side='right'caption='[[6vjk]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VJK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VJK 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]] 1.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</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=6vjk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vjk OCA], [https://pdbe.org/6vjk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vjk RCSB], [https://www.ebi.ac.uk/pdbsum/6vjk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vjk ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Although high affinity binding between streptavidin and biotin is widely exploited, the accompanying low rate of dissociation prevents its use in many applications where rapid ligand release is also required. To combine extremely tight and reversible binding, we have introduced disulfide bonds into opposite sides of a flexible loop critical for biotin binding, creating streptavidin muteins (M88 and M112) with novel disulfide-switchable binding properties. Crystal structures reveal how each disulfide exerts opposing effects on structure and function. Whereas the disulfide in M112 disrupts the closed conformation to increase koff, the disulfide in M88 stabilizes the closed conformation, decreasing koff 260-fold relative to streptavidin. The simple and efficient reduction of this disulfide increases koff 19,000-fold, thus creating a reversible redox-dependent switch with 70-fold faster dissociation kinetics than streptavidin. The facile control of disulfide formation in M88 will enable the development of many new applications requiring high affinity and reversible binding.

Engineering a disulfide-gated switch in streptavidin enables reversible binding without sacrificing binding affinity.,Marangoni JM, Wu SC, Fogen D, Wong SL, Ng KKS Sci Rep. 2020 Jul 27;10(1):12483. doi: 10.1038/s41598-020-69357-5. PMID:32719366<ref>PMID:32719366</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6vjk" style="background-color:#fffaf0;"></div>

==See Also==
*[[Avidin 3D structures|Avidin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Fogen D]]
[[Category: Marangoni JM]]
[[Category: Ng KKS]]
[[Category: Wong SL]]
[[Category: Wu SC]]