1ovb
From Proteopedia
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THE MECHANISM OF IRON UPTAKE BY TRANSFERRINS: THE STRUCTURE OF AN 18KD NII-DOMAIN FRAGMENT AT 2.3 ANGSTROMS RESOLUTION
Overview
The molecular structure of an iron-containing 18 kDa fragment of duck, ovotransferrin, obtained by proteolysis of the intact protein, has been, elucidated by protein crystallographic techniques at 2.3 A resolution., This structure supports a mechanism of iron uptake in the intact protein, whereby the binding of the synergistic (bi)carbonate anion is followed by, binding of the metal with the lobe in the open configuration. These stages, are then followed by domain closure in which the aspartic acid residue, plays a further key role, by forming an interdomain hydrogen-bond, interaction in addition to serving as a ligand to the iron. This essential, dual role is highlighted by model building studies on the C-terminal lobe, of a known human variant. In this variant a mutation of a glycine by an, arginine residue enables the aspartic acid to form an ion pair and reduce, its effectiveness for both metal binding and domain closure. The X-ray, structure of the 18 kDa fragment strongly suggests that the histidine, residue present at the iron binding site of the intact protein and arising, from the second interdomain connecting strand has been removed during the, preparative proteolysis.
About this Structure
1OVB is a Single protein structure of sequence from Anas sp. with FE and CO3 as ligands. Full crystallographic information is available from OCA.
Reference
The mechanism of iron uptake by transferrins: the structure of an 18 kDa NII-domain fragment from duck ovotransferrin at 2.3 A resolution., Lindley PF, Bajaj M, Evans RW, Garratt RC, Hasnain SS, Jhoti H, Kuser P, Neu M, Patel K, Sarra R, Strange R, Walton A, Acta Crystallogr D Biol Crystallogr. 1993 Mar 1;49(Pt 2):292-304. PMID:15299534
Page seeded by OCA on Tue Nov 20 23:13:32 2007
Categories: Anas sp. | Single protein | Kuser, P. | Lindley, P. | Sarra, R. | CO3 | FE | Iron transport protein
