1nft
OVOTRANSFERRIN, N-TERMINAL LOBE, IRON LOADED OPEN FORM
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OverviewOverview
Transferrins bind Fe3+ very tightly in a closed interdomain cleft by the, coordination of four protein ligands (Asp60, Tyr92, Tyr191, and His250 in, ovotransferrin N-lobe) and of a synergistic anion, physiologically, bidentate CO32-. Upon Fe3+ uptake, transferrins undergo a large scale, conformational transition: the apo structure with an opening of the, interdomain cleft is transformed into the closed holo structure, implying, initial Fe3+ binding in the open form. To solve the Fe3+-loaded, domain-opened structure, an ovotransferrin N-lobe crystal that had been, grown as the apo form was soaked with Fe3+-nitrilotriacetate, and its, structure was solved at 2.1 A resolution. The Fe3+-soaked form showed, almost exactly the same overall open structure as the iron-free apo form., The electron density map unequivocally proved the presence of an iron atom, with the coordination by the two protein ligands of Tyr92-OH and, Tyr191-OH. Other Fe3+ coordination sites are occupied by a, nitrilotriacetate anion, which is stabilized through the hydrogen bonds, with the peptide NH groups of Ser122, Ala123, and Gly124 and a side chain, group of Thr117. There is, however, no clear interaction between the, nitrilotriacetate anion and the synergistic anion binding site, Arg121.
About this StructureAbout this Structure
1NFT is a Single protein structure of sequence from Gallus gallus with SO4, FE and NTA as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Alternative structural state of transferrin. The crystallographic analysis of iron-loaded but domain-opened ovotransferrin N-lobe., Mizutani K, Yamashita H, Kurokawa H, Mikami B, Hirose M, J Biol Chem. 1999 Apr 9;274(15):10190-4. PMID:10187803
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