6iyh

X-ray sequence and high resolution crystal structure of Persian sturgeon methemoglobin

spinqualitylabelsall models 6iyh, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6iyh is a 2 chain structure with sequence from Acipenser persicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: HEM, PGO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1X8XL85_ACIPE Publication Abstract from PubMed Although there is a high sequence similarity between mammalian and fish hemoglobin (Hb), the oxidation and heme loss rates can vary greatly between them such that fish Hbs oxidise much more rapidly than mammalian Hbs. There is to date no sequence or structural data for any sturgeon Hb to reveal the level of autoxidation in these fish. In this study, novel high resolution X-ray sequences and crystal structures of methemoglobin (Met-Hb) from two sturgeon fish including Persian sturgeon (Acipenser percisus) and Starry sturgeon (Acipenser stellatus) belonging to the Caspian sea has been determined. A comprehensive sequence and structure comparison between these sturgeon Met-Hbs and a number of non-sturgeon and normal and sickle cell anaemia human Hb in varying heme states has been carried out highlighting (i) the structural variability in the heme propionate groups; (ii) the existence of certain residues or their displacement and shift in the heme pocket allowing entry of water molecules into the heme pocket; (iii) the importance of the number of water molecules in the heme pocket; (iv) the hydrogen bonding between oxygens of A and D propionate groups and that of waters in the heme pocket; and (v) the role of heme binding waters causing oxidative stress and heme autoxidation. Novel X-ray sequences and crystal structures of Persian and Starry sturgeon methemoglobins: Highlighting the role of heme pocket waters in causing autoxidation.,Seyedarabi A, Ariaeenejad S, Moosavi-Movahedi AA, Rayati S, Poursasan N, Asiaie N, Seraj Z, Mehraban F, Seyedarabi SE Biochim Biophys Acta Proteins Proteom. 2019 Mar 21;1867(6):586-594. doi:, 10.1016/j.bbapap.2019.03.008. PMID:30904680 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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