3u9j

Crystal structure of oxidized human FBXL5 hemerythrin like domain

spinqualitylabelsall models 3u9j, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3u9j is a 2 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 1.603Å Ligands: FE, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FBXL5_HUMAN Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. Upon high iron and oxygen level, it specifically recognizes and binds IREB2/IRP2, promoting its ubiquitination and degradation by the proteasome. Promotes ubiquitination and subsequent degradation of DCTN1/p150-glued. Publication Abstract from PubMed Iron sensing: The F-box and leucine-rich repeat containing protein FBXL5 is an iron sensor that regulates the ubiquitination of iron regulatory protein IRP2. Crystal structures of the iron-sensing hemetrythrin (Hr)-like domain of human FBXL5 (FBXL5 Hr) were determined in oxidized and reduced states. These structures revealed the mechanisms of iron sensing by FBXL5. The Structural Basis of Iron Sensing by the Human F-box Protein FBXL5.,Shu C, Sung MW, Stewart MD, Igumenova TI, Tan X, Li P Chembiochem. 2012 Apr 16;13(6):788-91. doi: 10.1002/cbic.201200043. PMID:22492618 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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