4FZP

Crystal Structure of the uranyl binding protein complexed with uranyl

Summary for 4FZP

• Entry DOI: 10.2210/pdb4fzp/pdb
• Related: 4FZO
• Descriptor: uranyl binding protein, URANYL (VI) ION (3 entities in total)
• Functional Keywords: uranyl binding, unknown function
• Biological source: Methanothermobacter thermautotrophicus
• Total number of polymer chains: 2
• Total formula weight: 19625.43

Authors

Zhou, L.,Zhang, L.,He, C. (deposition date: 2012-07-06, release date: 2013-12-11, Last modification date: 2024-02-28)

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

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: 24557139
DOI: 10.1038/nchem.1856

Experimental method

X-RAY DIFFRACTION (1.29 Å)