View source for 6fh8


==E. coli surface display of streptavidin for directed evolution of an allylic deallocase==
<StructureSection load='6fh8' size='340' side='right'caption='[[6fh8]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6fh8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FH8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FH8 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]] 1.64&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=JCT:biotinylated+ruthenium+cyclopentadienide'>JCT</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=6fh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fh8 OCA], [https://pdbe.org/6fh8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fh8 RCSB], [https://www.ebi.ac.uk/pdbsum/6fh8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fh8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://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 hereafter) combine attractive features of both homogeneous catalysts and enzymes and offer the potential to implement new-to-nature reactions in living organisms. Herein we present an E. coli surface display platform for streptavidin (Sav hereafter) relying on an Lpp-OmpA anchor. The system was used for the high throughput screening of a bioorthogonal CpRu-based artificial deallylase (ADAse) that uncages an allylcarbamate-protected aminocoumarin 1. Two rounds of directed evolution afforded the double mutant S112M-K121A that displayed a 36-fold increase in surface activity vs. cellular background and a 5.7-fold increased in vitro activity compared to the wild type enzyme. The crystal structure of the best ADAse reveals the importance of mutation S112M to stabilize the cofactor conformation inside the protein.

E. coli surface display of streptavidin for directed evolution of an allylic deallylase.,Heinisch T, Schwizer F, Garabedian B, Csibra E, Jeschek M, Vallapurackal J, Pinheiro VB, Marliere P, Panke S, Ward TR Chem Sci. 2018 May 24;9(24):5383-5388. doi: 10.1039/c8sc00484f. eCollection 2018 , Jun 28. PMID:30079176<ref>PMID:30079176</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6fh8" style="background-color:#fffaf0;"></div>

==See Also==
*[[Avidin 3D structures|Avidin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces avidinii]]
[[Category: Csibra E]]
[[Category: Garabedian B]]
[[Category: Heinisch T]]
[[Category: Jeschek M]]
[[Category: Marliere P]]
[[Category: Panke S]]
[[Category: Pinheiro Bernhardes V]]
[[Category: Schwizer F]]
[[Category: Ward TR]]