4FZO
Crystal Structure of the apo-form uranyl binding protein
Summary for 4FZO
| Entry DOI | 10.2210/pdb4fzo/pdb |
| Related | 4FZP |
| Descriptor | uranyl binding protein (2 entities in total) |
| Functional Keywords | uranyl binding, uranyl, unknown function |
| Biological source | Methanothermobacter thermautotrophicus |
| Total number of polymer chains | 2 |
| Total formula weight | 19085.37 |
| Authors | |
| Primary citation | Zhou, L.,Bosscher, M.,Zhang, C.,Ozcubukcu, S.,Zhang, L.,Zhang, W.,Li, C.J.,Liu, J.,Jensen, M.P.,Lai, L.,He, C. A protein engineered to bind uranyl selectively and with femtomolar affinity. Nat Chem, 6:236-241, 2014 Cited by PubMed Abstract: Uranyl (UO2(2+)), the predominant aerobic form of uranium, is present in the ocean at a concentration of ~3.2 parts per 10(9) (13.7 nM); however, the successful enrichment of uranyl from this vast resource has been limited by the high concentrations of metal ions of similar size and charge, which makes it difficult to design a binding motif that is selective for uranyl. Here we report the design and rational development of a uranyl-binding protein using a computational screening process in the initial search for potential uranyl-binding sites. The engineered protein is thermally stable and offers very high affinity and selectivity for uranyl with a Kd of 7.4 femtomolar (fM) and >10,000-fold selectivity over other metal ions. We also demonstrated that the uranyl-binding protein can repeatedly sequester 30-60% of the uranyl in synthetic sea water. The chemical strategy employed here may be applied to engineer other selective metal-binding proteins for biotechnology and remediation applications. PubMed: 24557139DOI: 10.1038/nchem.1856 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
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