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==WILDTYPE CORE-STREPTAVIDIN WITH a conjugated BIOTINYLATED PYRROLIDINE II== | ==WILDTYPE CORE-STREPTAVIDIN WITH a conjugated BIOTINYLATED PYRROLIDINE II== | ||
<StructureSection load='7nlv' size='340' side='right'caption='[[7nlv]]' scene=''> | <StructureSection load='7nlv' size='340' side='right'caption='[[7nlv]], [[Resolution|resolution]] 1.29Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NLV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NLV FirstGlance]. <br> | <table><tr><td colspan='2'>[[7nlv]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NLV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NLV FirstGlance]. <br> | ||
</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=7nlv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nlv OCA], [https://pdbe.org/7nlv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nlv RCSB], [https://www.ebi.ac.uk/pdbsum/7nlv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nlv ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UJE:5-((3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)-N-((S)-pyrrolidin-3-yl)pentanamide'>UJE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6zyt|6zyt]], [[6gh7|6gh7]]</div></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=7nlv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nlv OCA], [https://pdbe.org/7nlv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nlv RCSB], [https://www.ebi.ac.uk/pdbsum/7nlv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nlv ProSAT]</span></td></tr> | |||
</table> | </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 == | |||
Here, we combine the use of host screening, protein crystallography and QM/MM molecular dynamics simulations to investigate how the protein structure affects iminium catalysis by biotinylated secondary amines in a model 1,4 conjugate addition reaction. Monomeric streptavidin (M-Sav) lacks a quaternary structure and the solvent-exposed reaction site resulted in poor product conversion in the model reaction with low enantio- and regioselectivities. These parameters were much improved when the tetrameric host T-Sav was used; indeed, residues at the symmetrical subunit interface were proven to be critical for catalysis through a mutagenesis study. The use of QM/MM simulations and the asymmetric dimeric variant D-Sav revealed that both Lys121 residues which are located in the hosting and neighboring subunits play a critical role in controlling the stereoselectivity and reactivity. Lastly, the D-Sav template, though providing a lower conversion than that of the symmetric tetrameric counterpart, is likely a better starting point for future protein engineering because each surrounding residue within the asymmetric scaffold can be refined for secondary amine catalysis. | |||
The role of streptavidin and its variants in catalysis by biotinylated secondary amines.,Nodling AR, Santi N, Castillo R, Lipka-Lloyd M, Jin Y, Morrill LC, Swiderek K, Moliner V, Luk LYP Org Biomol Chem. 2021 Dec 8;19(47):10424-10431. doi: 10.1039/d1ob01947c. PMID:34825690<ref>PMID:34825690</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7nlv" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Jin Y]] | [[Category: Jin, Y]] | ||
[[Category: Luk | [[Category: Luk, L Y.P]] | ||
[[Category: Nodling | [[Category: Nodling, A R]] | ||
[[Category: Rizkallah P]] | [[Category: Rizkallah, P]] | ||
[[Category: Santi N]] | [[Category: Santi, N]] | ||
[[Category: Tsai | [[Category: Tsai, Y H]] | ||
[[Category: Artificial enzyme]] | |||
[[Category: Beta-barrel]] | |||
[[Category: Biotin-binding protein]] | |||
[[Category: De novo protein]] | |||
[[Category: Streptavidin]] | |||
Revision as of 10:21, 9 March 2022
WILDTYPE CORE-STREPTAVIDIN WITH a conjugated BIOTINYLATED PYRROLIDINE IIWILDTYPE CORE-STREPTAVIDIN WITH a conjugated BIOTINYLATED PYRROLIDINE II
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 PubMedHere, we combine the use of host screening, protein crystallography and QM/MM molecular dynamics simulations to investigate how the protein structure affects iminium catalysis by biotinylated secondary amines in a model 1,4 conjugate addition reaction. Monomeric streptavidin (M-Sav) lacks a quaternary structure and the solvent-exposed reaction site resulted in poor product conversion in the model reaction with low enantio- and regioselectivities. These parameters were much improved when the tetrameric host T-Sav was used; indeed, residues at the symmetrical subunit interface were proven to be critical for catalysis through a mutagenesis study. The use of QM/MM simulations and the asymmetric dimeric variant D-Sav revealed that both Lys121 residues which are located in the hosting and neighboring subunits play a critical role in controlling the stereoselectivity and reactivity. Lastly, the D-Sav template, though providing a lower conversion than that of the symmetric tetrameric counterpart, is likely a better starting point for future protein engineering because each surrounding residue within the asymmetric scaffold can be refined for secondary amine catalysis. The role of streptavidin and its variants in catalysis by biotinylated secondary amines.,Nodling AR, Santi N, Castillo R, Lipka-Lloyd M, Jin Y, Morrill LC, Swiderek K, Moliner V, Luk LYP Org Biomol Chem. 2021 Dec 8;19(47):10424-10431. doi: 10.1039/d1ob01947c. PMID:34825690[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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