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| | <StructureSection load='5f2b' size='340' side='right'caption='[[5f2b]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='5f2b' size='340' side='right'caption='[[5f2b]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5f2b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/As_4.1583 As 4.1583]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F2B OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5F2B FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5f2b]] 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=5F2B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F2B FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9RU:[1-[4-[[5-[(3~{a}~{S},4~{S},6~{a}~{R})-2-oxidanylidene-1,3,3~{a},4,6,6~{a}-hexahydrothieno[3,4-d]imidazol-4-yl]pentanoylamino]methyl]-2,6-dimethyl-phenyl]-3-(2,4,6-trimethylphenyl)-4,5-dihydroimidazol-1-ium-2-yl]-bis(chloranyl)ruthenium'>9RU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5f2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f2b OCA], [http://pdbe.org/5f2b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f2b RCSB], [http://www.ebi.ac.uk/pdbsum/5f2b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f2b ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9RU:[1-[4-[[5-[(3~{a}~{S},4~{S},6~{a}~{R})-2-oxidanylidene-1,3,3~{a},4,6,6~{a}-hexahydrothieno[3,4-d]imidazol-4-yl]pentanoylamino]methyl]-2,6-dimethyl-phenyl]-3-(2,4,6-trimethylphenyl)-4,5-dihydroimidazol-1-ium-2-yl]-bis(chloranyl)ruthenium'>9RU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5f2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f2b OCA], [https://pdbe.org/5f2b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f2b RCSB], [https://www.ebi.ac.uk/pdbsum/5f2b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f2b ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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). | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: As 4 1583]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Heinisch, T]] | + | [[Category: Streptomyces avidinii]] |
| - | [[Category: Jeschek, M]] | + | [[Category: Heinisch T]] |
| - | [[Category: Panke, S]] | + | [[Category: Jeschek M]] |
| - | [[Category: Reuter, R]] | + | [[Category: Panke S]] |
| - | [[Category: Trindler, C]] | + | [[Category: Reuter R]] |
| - | [[Category: Ward, T R]] | + | [[Category: Trindler C]] |
| - | [[Category: Beta barrel]]
| + | [[Category: Ward TR]] |
| - | [[Category: Biotin-binding protein]]
| + | |
| - | [[Category: Metathesis]]
| + | |
| - | [[Category: Organometallic complex]]
| + | |
| Structural highlights
Function
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).
Publication Abstract from PubMed
The field of biocatalysis has advanced from harnessing natural enzymes to using directed evolution to obtain new biocatalysts with tailor-made functions. Several tools have recently been developed to expand the natural enzymatic repertoire with abiotic reactions. For example, artificial metalloenzymes, which combine the versatile reaction scope of transition metals with the beneficial catalytic features of enzymes, offer an attractive means to engineer new reactions. Three complementary strategies exist: repurposing natural metalloenzymes for abiotic transformations; in silico metalloenzyme (re-)design; and incorporation of abiotic cofactors into proteins. The third strategy offers the opportunity to design a wide variety of artificial metalloenzymes for non-natural reactions. However, many metal cofactors are inhibited by cellular components and therefore require purification of the scaffold protein. This limits the throughput of genetic optimization schemes applied to artificial metalloenzymes and their applicability in vivo to expand natural metabolism. Here we report the compartmentalization and in vivo evolution of an artificial metalloenzyme for olefin metathesis, which represents an archetypal organometallic reaction without equivalent in nature. Building on previous work on an artificial metallohydrolase, we exploit the periplasm of Escherichia coli as a reaction compartment for the 'metathase' because it offers an auspicious environment for artificial metalloenzymes, mainly owing to low concentrations of inhibitors such as glutathione, which has recently been identified as a major inhibitor. This strategy facilitated the assembly of a functional metathase in vivo and its directed evolution with substantially increased throughput compared to conventional approaches that rely on purified protein variants. The evolved metathase compares favourably with commercial catalysts, shows activity for different metathesis substrates and can be further evolved in different directions by adjusting the workflow. Our results represent the systematic implementation and evolution of an artificial metalloenzyme that catalyses an abiotic reaction in vivo, with potential applications in, for example, non-natural metabolism.
Directed evolution of artificial metalloenzymes for in vivo metathesis.,Jeschek M, Reuter R, Heinisch T, Trindler C, Klehr J, Panke S, Ward TR Nature. 2016 Aug 29. doi: 10.1038/nature19114. PMID:27571282[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jeschek M, Reuter R, Heinisch T, Trindler C, Klehr J, Panke S, Ward TR. Directed evolution of artificial metalloenzymes for in vivo metathesis. Nature. 2016 Aug 29. doi: 10.1038/nature19114. PMID:27571282 doi:http://dx.doi.org/10.1038/nature19114
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