6DYK
Iron- and Nitric Oxide-bound structure of the engineered cyt b562 variant, CH3Y*
Summary for 6DYK
| Entry DOI | 10.2210/pdb6dyk/pdb |
| Related | 6DY4 6DY6 6DY8 6DYB 6DYC 6DYD 6DYE 6DYF 6DYG 6DYH 6DYI 6DYJ |
| Descriptor | Soluble cytochrome b562, FE (III) ION, NITRIC OXIDE, ... (4 entities in total) |
| Functional Keywords | designed protein, 4-helix bundle, metal binding protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 4 |
| Total formula weight | 47893.20 |
| Authors | Tezcan, F.A.,Rittle, J. (deposition date: 2018-07-01, release date: 2019-04-24, Last modification date: 2024-10-30) |
| Primary citation | Rittle, J.,Field, M.J.,Green, M.T.,Tezcan, F.A. An efficient, step-economical strategy for the design of functional metalloproteins. Nat.Chem., 11:434-441, 2019 Cited by PubMed Abstract: The bottom-up design and construction of functional metalloproteins remains a formidable task in biomolecular design. Although numerous strategies have been used to create new metalloproteins, pre-existing knowledge of the tertiary and quaternary protein structure is often required to generate suitable platforms for robust metal coordination and activity. Here we report an alternative and easily implemented approach (metal active sites by covalent tethering or MASCoT) in which folded protein building blocks are linked by a single disulfide bond to create diverse metal coordination environments within evolutionarily naive protein-protein interfaces. Metalloproteins generated using this strategy uniformly bind a wide array of first-row transition metal ions (Mn, Fe, Co, Ni, Cu, Zn and vanadyl) with physiologically relevant thermodynamic affinities (dissociation constants ranging from 700 nM for Mn to 50 fM for Cu). MASCoT readily affords coordinatively unsaturated metal centres-including a penta-His-coordinated non-haem Fe site-and well-defined binding pockets that can accommodate modifications and enable coordination of exogenous ligands such as nitric oxide to the interfacial metal centre. PubMed: 30778140DOI: 10.1038/s41557-019-0218-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.955 Å) |
Structure validation
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