“Anion clamp” allows flexible protein to impose coordination geometry on metal ions

2015 ◽  
Vol 51 (37) ◽  
pp. 7867-7870 ◽  
Author(s):  
Minji Wang ◽  
Tsz Pui Lai ◽  
Li Wang ◽  
Hongmin Zhang ◽  
Nan Yang ◽  
...  
Keyword(s):  
Metal Ions ◽  
Human Serum ◽  
Metal Binding ◽  
Binding Pocket ◽  
Serum Transferrin ◽  
Coordination Geometry ◽  
Human Serum Transferrin ◽  
Lanthanide Ion ◽  
X Ray ◽  
Flexible Protein

X-ray crystal structures of human serum transferrin (77 kDa) with YbIII or FeIII bound to the C-lobe and malonate as the synergistic anion show that the large YbIII ion causes the expansion of the metal binding pocket while octahedral metal coordination geometry is preserved, an unusual geometry for a lanthanide ion.

scholarly journals Flexibility of the Coordination Geometry at the N-Site of Cu(II)2 Human Serum-Transferrin Induced by the Different Orientations of Arg124

2015 ◽  
Vol 38 (3) ◽  
pp. 358-364 ◽  
Author(s):  
Toshiyuki Hata ◽  
Yu Shibata ◽  
Miku Okano ◽  
Asako Kodera ◽  
Misato Ueda ◽  
...  
Keyword(s):  
Human Serum ◽  
Serum Transferrin ◽  
Coordination Geometry ◽  
Human Serum Transferrin

Effects of Mutations of Aspartic Acid 63 on the Metal-Binding Properties of the Recombinant N-Lobe of Human Serum Transferrin†

Biochemistry ◽  
1997 ◽  
Vol 36 (18) ◽  
pp. 5522-5528 ◽  
Author(s):  
Qing-Yu He ◽  
Anne B. Mason ◽  
Robert C. Woodworth ◽  
Beatrice M. Tam ◽  
Toby Wadsworth ◽  
...  
Keyword(s):  
Human Serum ◽  
Aspartic Acid ◽  
Metal Binding ◽  
Serum Transferrin ◽  
Binding Properties ◽  
Human Serum Transferrin

A Density Functional Theory Study of the Iron-Binding Site of Human Serum Transferrin

2004 ◽  
Vol 57 (12) ◽  
pp. 1219 ◽  
Author(s):  
David Rinaldo ◽  
Martin J. Field
Keyword(s):  
Human Serum ◽  
Binding Site ◽  
Conformational Changes ◽  
Metal Binding ◽  
Density Functional ◽  
Release Mechanism ◽  
Serum Transferrin ◽  
Iron Binding ◽  
Iron Release ◽  
Human Serum Transferrin

Human serum transferrin binds ferric ions with high affinity in the blood stream and releases them into cells by a process involving receptor-mediated endocytosis and a decrease in pH. The iron-release mechanism is unclear but protonation events and conformational changes are known to be important. In this study, we investigate properties of the iron-binding site theoretically. Our results suggest that an equatorial histidine could be in its histidinate form when bound to iron at neutral and high pH and that protonation of an axial tyrosine is a key event in iron release. Support for this mechanism from other metal-binding enzymes is also presented.

scholarly journals Trp128Tyr mutation in the N-lobe of recombinant human serum transferrin: 1H- and 15N-NMR and metal binding studies

1997 ◽  
Vol 10 (5) ◽  
pp. 583-591 ◽  
Author(s):  
E. J. Beatty ◽  
M. C. Cox ◽  
T. A. Frenkiel ◽  
Q. Y. He ◽  
A. B. Mason ◽  
...  
Keyword(s):  
Human Serum ◽  
Metal Binding ◽  
15N Nmr ◽  
Serum Transferrin ◽  
Binding Studies ◽  
Human Serum Transferrin

scholarly journals Density Functional Theory Study on Metal-Binding Energies for Human Serum Transferrin-Metal Complexes

2012 ◽  
Vol 2012 ◽  
pp. 1-5 ◽  
Author(s):  
Tetsuya Sakajiri ◽  
Hirofumi Yajima ◽  
Takaki Yamamura
Keyword(s):  
Density Functional Theory ◽  
Human Serum ◽  
Metal Binding ◽  
Density Functional ◽  
Conformational Transition ◽  
Binding Energies ◽  
Serum Transferrin ◽  
Functional Theory ◽  
Human Serum Transferrin ◽  
Solvation Energies

The absolute values of the metal-binding energies of human serum transferrin (Tf) N-lobe, |ΔE|, were calculated using the density functional theory and were found to increase in magnitude in the following order: Fe(III)>Ga(III)>Al(III)>Cu(II)>Zn(II)>Ni(II). The calculated energies were well correlated with the logarithmic values of the reported metal-binding constants of Tf, which had been experimentally determined, with a correlation coefficient of 0.96. In the estimation of the binding energies, the solvation energies (solvent effect) of free metal ions were a very important factor. The results provide a theoretical explanation for the binding of Fe(III) to Tf, which produces sufficient energy to induce a conformational transition of the Tf molecule, making it possible to interact with Tf receptor 1.

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