5l3y: Difference between revisions
New page: '''Unreleased structure''' The entry 5l3y is ON HOLD Authors: Mann, S.I., Heinisch, T., Weitz, A.C., Hendrich, M.R., Ward, T.R., Borovik, A.S. Description: Designed Artificial Cupredox... |
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The | ==Designed Artificial Cupredoxins== | ||
<StructureSection load='5l3y' size='340' side='right'caption='[[5l3y]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5l3y]] 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=5L3Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5L3Y 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]] 1.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU6:[CUII(BIOT-ET-DPEA)]2+'>CU6</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=5l3y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l3y OCA], [https://pdbe.org/5l3y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l3y RCSB], [https://www.ebi.ac.uk/pdbsum/5l3y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l3y 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 == | |||
Cupredoxins are electron-transfer proteins that have active sites containing a mononuclear Cu center with an unusual trigonal monopyramidal structure (Type 1 Cu). A single Cu-Scys bond is present within the trigonal plane that is responsible for its unique physical properties. We demonstrate that a cysteine-containing variant of streptavidin (Sav) can serve as a protein host to model the structure and properties of Type 1 Cu sites. A series of artificial Cu proteins are described that rely on Sav and a series of biotinylated synthetic Cu complexes. Optical and EPR measurements highlight the presence of a Cu-Scys bond, and XRD analysis provides structural evidence. We further provide evidence that changes in the linker between the biotin and Cu complex within the synthetic constructs allows for small changes in the placement of Cu centers within Sav that have dramatic effects on the structural and physical properties of the resulting artificial metalloproteins. These findings highlight the utility of the biotin-Sav technology as an approach for simulating active sites of metalloproteins. | |||
Modular Artificial Cupredoxins.,Mann SI, Heinisch T, Weitz AC, Hendrich MP, Ward TR, Borovik AS J Am Chem Soc. 2016 Jul 14. PMID:27385206<ref>PMID:27385206</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5l3y" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: Mann | *[[Avidin 3D structures|Avidin 3D structures]] | ||
[[Category: Ward | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptomyces avidinii]] | |||
[[Category: Borovik AS]] | |||
[[Category: Heinisch T]] | |||
[[Category: Hendrich MR]] | |||
[[Category: Mann SI]] | |||
[[Category: Ward TR]] | |||
[[Category: Weitz AC]] | |||
Latest revision as of 19:06, 4 October 2023
Designed Artificial CupredoxinsDesigned Artificial Cupredoxins
Structural highlights
FunctionSAV_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 PubMedCupredoxins are electron-transfer proteins that have active sites containing a mononuclear Cu center with an unusual trigonal monopyramidal structure (Type 1 Cu). A single Cu-Scys bond is present within the trigonal plane that is responsible for its unique physical properties. We demonstrate that a cysteine-containing variant of streptavidin (Sav) can serve as a protein host to model the structure and properties of Type 1 Cu sites. A series of artificial Cu proteins are described that rely on Sav and a series of biotinylated synthetic Cu complexes. Optical and EPR measurements highlight the presence of a Cu-Scys bond, and XRD analysis provides structural evidence. We further provide evidence that changes in the linker between the biotin and Cu complex within the synthetic constructs allows for small changes in the placement of Cu centers within Sav that have dramatic effects on the structural and physical properties of the resulting artificial metalloproteins. These findings highlight the utility of the biotin-Sav technology as an approach for simulating active sites of metalloproteins. Modular Artificial Cupredoxins.,Mann SI, Heinisch T, Weitz AC, Hendrich MP, Ward TR, Borovik AS J Am Chem Soc. 2016 Jul 14. PMID:27385206[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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