5K68

Designed Artificial Cupredoxins

Summary for 5K68

• Entry DOI: 10.2210/pdb5k68/pdb
• Descriptor: Streptavidin, [CuII(biot-bu-dpea)]2+ (3 entities in total)
• Functional Keywords: beta-barrel, biotin binding protein, tetramer, cupredoxin, artificial metalloprotein, copper protein
• Biological source: Streptomyces avidinii
• Total number of polymer chains: 1
• Total formula weight: 17174.35

Authors

Mann, S.I.,Heinisch, T.,Weitz, A.C.,Hendrich, M.R.,Ward, T.R.,Borovik, A.S. (deposition date: 2016-05-24, release date: 2016-07-20, Last modification date: 2024-01-10)

Primary citation

Mann, S.I.,Heinisch, T.,Weitz, A.C.,Hendrich, M.P.,Ward, T.R.,Borovik, A.S.
Modular Artificial Cupredoxins.
J.Am.Chem.Soc., 138:9073-9076, 2016

PubMed Abstract: 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.

PubMed: 27385206
DOI: 10.1021/jacs.6b05428

Experimental method

X-RAY DIFFRACTION (1.4 Å)