6t2z

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'''Unreleased structure'''
 
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The entry 6t2z is ON HOLD until Paper Publication
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==Streptavidin variants harbouring an artificial organocatalyst based cofactor==
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<StructureSection load='6t2z' size='340' side='right'caption='[[6t2z]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6t2z]] is a 2 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=6T2Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T2Z FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HL9:5-[(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]-~{N}-(1-pyridin-4-ylpiperidin-4-yl)pentanamide'>HL9</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6t2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t2z OCA], [https://pdbe.org/6t2z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t2z RCSB], [https://www.ebi.ac.uk/pdbsum/6t2z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t2z ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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An artificial cofactor based on an organocatalyst embedded in a protein has been used to conduct the Baylis-Hillman reaction in a buffered system. As protein host, we chose streptavidin, as it can be easily crystallized and thereby supports the design process. The protein host around the cofactor was rationally designed on the basis of high-resolution crystal structures obtained after each variation of the amino acid sequence. Additionally, DFT-calculated intermediates and transition states were used to rationalize the observed activity. Finally, repeated cycles of structure determination and redesign led to a system with an up to one order of magnitude increase in activity over the bare cofactor and to the most active proteinogenic catalyst for the Baylis-Hillman reaction known today.
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Authors: Lechner, H., Hocker, B.
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An Artificial Cofactor Catalyzing the Baylis-Hillman Reaction with Designed Streptavidin as Protein Host*.,Lechner H, Emann VR, Breuning M, Hocker B Chembiochem. 2021 Jan 5. doi: 10.1002/cbic.202000880. PMID:33400831<ref>PMID:33400831</ref>
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Description: Streptavidin variants harbouring an artificial organocatalyst based cofactor
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Lechner, H]]
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<div class="pdbe-citations 6t2z" style="background-color:#fffaf0;"></div>
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[[Category: Hocker, B]]
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==See Also==
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*[[Avidin 3D structures|Avidin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Streptomyces avidinii]]
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[[Category: Hocker B]]
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[[Category: Lechner H]]

Current revision

Streptavidin variants harbouring an artificial organocatalyst based cofactor

PDB ID 6t2z

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