5wbc

Designed Artificial Cupredoxins - WT

spinqualitylabelsall models 5wbc, resolution 1.72Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5wbc is a 1 chain structure. This structure supersedes the now removed PDB entry 5k49. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, CU6, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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