1ovb

THE MECHANISM OF IRON UPTAKE BY TRANSFERRINS: THE STRUCTURE OF AN 18KD NII-DOMAIN FRAGMENT AT 2.3 ANGSTROMS RESOLUTION

spinqualitylabelsall models 1ovb, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ovb is a 1 chain structure with sequence from Anas sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: CO3, FE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TRFE_ANAPL Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation. Ovotransferrin has a bacteriostatic function. Its concentration in avian egg is the highest concentration of any transferrin in vivo (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transferrin 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA