The HBx protein from hepatitis B virus coordinates a redox-active Fe-S cluster
Chie Ueda, Michelle Langton, Jiahua Chen, Maria‐Eirini Pandelia
Abstract
couple (-520 mV) suggests that electron transfer may not be likely in the cell. Collectively, our findings identify HBx as an Fe-S protein with striking similarities to Fe-S scaffold proteins both in cluster type and reductive transformation. An Fe-S cluster in HBx offers new insights into its previously unknown molecular properties and sets the stage for deciphering the roles of HBx-associated iron (mis)regulation and reactive oxygen species in the context of liver tumorigenesis.
Topics & Concepts
HBxChemistryContext (archaeology)Hepatocellular carcinomaCluster (spacecraft)RedoxHepatitis B virusScaffold proteinCarcinogenesisBiochemistryCombinatorial chemistryBiologyVirusVirologyCancer researchInorganic chemistryGeneSignal transductionComputer scienceProgramming languagePaleontologyPorphyrin Metabolism and DisordersFolate and B Vitamins ResearchHepatitis B Virus Studies