Journal
SCIENTIFIC REPORTS
Volume 2, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/srep00999
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Funding
- Research Grants Council of Hong Kong [HKU7049/09P, N_HKU752/09, HKU7053/10P]
- Croucher Foundation
- Strategic Research Theme of the University of Hong Kong
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Human serum transferrin (hTF) binds Fe(III) tightly but reversibly, and delivers it to cells via a receptor-mediated endocytosis process. The metal-binding and release result in significant conformational changes of the protein. Here, we report the crystal structures of diferric-hTF (FeNFeC-hTF) and bismuth-bound hTF (BiNFeC-hTF) at 2.8 and 2.4 angstrom resolutions respectively. Notably, the N-lobes of both structures exhibit unique partially-opened'' conformations between those of the apo-hTF and holo-hTF. Fe(III) and Bi(III) in the N-lobe coordinate to, besides anions, only two (Tyr95 and Tyr188) and one (Tyr188) tyrosine residues, respectively, in contrast to four residues in the holo-hTF. The C-lobe of both structures are fully closed with iron coordinating to four residues and a carbonate. The structures of hTF observed here represent key conformers captured in the dynamic nature of the transferrin family proteins and provide a structural basis for understanding the mechanism of metal uptake and release in transferrin families.
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