6uj6 | pdb_00006uj6

X-ray Crystal Structure of Chromium-transferrin with Synergistic Anion Malonate

spinqualitylabelsall models 6uj6, resolution 2.68Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6uj6 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.68Å Ligands: BCT, CR, GOL, MLI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease TRFE_HUMAN Defects in TF are the cause of atransferrinemia (ATRAF) [MIM:209300. Atransferrinemia is rare autosomal recessive disorder characterized by iron overload and hypochromic anemia. Function TRFE_HUMAN 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. Publication Abstract from PubMed Transferrin, the Fe(III) transport protein in mammalian blood, has been suggested to also serve as a Cr(III) transporter and as part of a Cr(III) detoxification system; however, the structure of the metal-binding sites has never been fully elucidated with bound Cr(III). Chromium(III)-transferrin was crystallized in the presence of the synergistic anion malonate. In the crystals, the protein exists with a closed C-terminal lobe containing a Cr(III) ion and an open, unoccupied N-terminal lobe. The overall structure and the metal ion environments are extremely similar to those of Fe(III)- and Ti(IV)-containing transferrin crystallized under comparable conditions. The octahedral coordination about the Cr(III) is comprised of four ligands provided by the protein (two tyrosine residues, a histidine residue, and an aspartate residue) and a chelating malonate anion. This represents the first crystal structure of a Cr(III)-containing protein that binds Cr(III) as part of its physiological function. X-ray structure of chromium(III)-containing transferrin: First structure of a physiological Cr(III)-binding protein.,Petersen CM, Edwards KC, Gilbert NC, Vincent JB, Thompson MK J Inorg Biochem. 2020 Sep;210:111101. doi: 10.1016/j.jinorgbio.2020.111101. Epub , 2020 May 23. PMID:32650146 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transferrin 3D structures

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