6WZA
Ni-bound structure of an engineered metal-dependent protein trimer, TriCyt1
Summary for 6WZA
| Entry DOI | 10.2210/pdb6wza/pdb |
| Descriptor | Soluble cytochrome b562, HEME C, NICKEL (II) ION, ... (7 entities in total) |
| Functional Keywords | four-helix bundle, metalloprotein trimer, metal binding protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 3 |
| Total formula weight | 38159.37 |
| Authors | Tezcan, F.A.,Kakkis, A. (deposition date: 2020-05-13, release date: 2020-09-16, Last modification date: 2024-11-06) |
| Primary citation | Kakkis, A.,Gagnon, D.,Esselborn, J.,Britt, R.D.,Tezcan, F.A. Metal-Templated Design of Chemically Switchable Protein Assemblies with High-Affinity Coordination Sites. Angew.Chem.Int.Ed.Engl., 59:21940-21944, 2020 Cited by PubMed Abstract: To mimic a hypothetical pathway for protein evolution, we previously tailored a monomeric protein (cyt cb ) for metal-mediated self-assembly, followed by re-design of the resulting oligomers for enhanced stability and metal-based functions. We show that a single hydrophobic mutation on the cyt cb surface drastically alters the outcome of metal-directed oligomerization to yield a new trimeric architecture, (TriCyt1) This nascent trimer was redesigned into second and third-generation variants (TriCyt2) and (TriCyt3) with increased structural stability and preorganization for metal coordination. The three TriCyt variants combined furnish a unique platform to 1) provide tunable coupling between protein quaternary structure and metal coordination, 2) enable the construction of metal/pH-switchable protein oligomerization motifs, and 3) generate a robust metal coordination site that can coordinate all mid-to-late first-row transition-metal ions with high affinity. PubMed: 32830423DOI: 10.1002/anie.202009226 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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